



@article {2281,
	title = {Adhesion of human leukocytes on mixtures of hydroxyl- and methyl-terminated self-assembled monolayers: Effect of blood protein adsorption},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {93},
	year = {2010},
	note = {Cited By (since 1996): 4Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.32480PubMed ID: 19484768Language of Original Document: EnglishCorrespondence Address: Barbosa, J. N.; Divis{\~a}o de Biomateriais, INEB-Instituto de Engenharia Biom{\'e}dica, Universidade do Porto, Porto 4150-180, Portugal; email: judite@ineb.up.ptChemicals/CAS: Blood Proteins; Gold, 7440-57-5; Hydroxyl Radical, 3352-57-6References: Brodbeck, W.G., Nakayama, Y., Matsuda, T., Colton, E., Ziats, N.P., Anderson, J.M., Biomaterial surface chemistry dictates adherent monocyte/macrophage cytokine expression in vitro (2002) Cytokine, 18, pp. 311-319;Kao, W.Y.J., Evaluation of leukocyte adhesion on polyurethanes: The effects of shear stress and blood proteins (2000) Biomaterials, 21, pp. 2295-2303; 
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Barbosa, J.N., Madureira, P., Barbosa, M.A., Aguas, A.P., The attraction of Mac-1(+) phagocytes during acute inflammation by methyl-coated self-assembled monolayers (2005) Biomaterials, 26, pp. 3021-3027
},
	month = {2010///},
	pages = {12 - 19},
	abstract = {The adhesion of human leukocytes to nanostructured surfaces with different chemical properties and the effect of protein adsorption were investigated. Selfassembled monolayers (SAMs) prepared with mixtures of methyl- and hydroxyl-terminated alkanethiols in different percentages on gold were used. The surfaces were preimmersed in distinct protein solutions (human serum albumin, human fibrinogen, and autologous plasma). Adherent leukocytes were analyzed both by light and SEM. SAMs submitted to pre-immersion in plasma presented higher numbers of adherent leukocytes in the pure OH-terminated SAM, whereas methyl-terminated surfaces accounted for the lowest number of adherent cells. We observed a general increase in the number of adherent human leukocytes as the percentage of OH groups on the surface of the SAMs increased for all the pre-immersion conditions investigated. The number of adherent human leukocytes is highly influenced by the pre-immersion conditions used, and this observation is particularly relevant in the case of the methyl-terminated SAMs. The results obtained demonstrate that surface chemistry has a major influence in leukocyte adhesion to biomaterials, and that pre-immersion in protein solutions has a determinant effect in leukocyte adhesion. {\textcopyright} 2009 Wiley Periodicals, Inc.},
	keywords = {Adherent cells, Adhesion, Adsorption, Alkanethiols, article, Biological materials, biomaterial, Blood protein adsorption, Blood Proteins, cell adhesion, Cell Count, Chemical properties, gold, human, human cell, Human leukocytes, Human serum albumins, Humans, hydroxyl group, Hydroxyl Radical, Hydroxyl-terminated, immersion, Inflammatory response, leukocyte adherence, Leukocyte adhesion, Leukocytes, Nanostructured materials, Nanostructured surface, Nanostructured surfaces, OH group, Protein adsorption, protein blood level, Protein solution, Proteins, Sams, Scanning electron microscopy, Self assembled monolayers, Self-assembled monolayers, SEM, Surface chemistry, Surface Properties},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77649225392\&partnerID=40\&md5=0b35403e1b98581c557435b6cf7a8286},
	author = {Barbosa, J.N. and Martins, M.C.L. and Freitas, S.C. and Gon{\c c}alves, I.C. and {\'A}guas, A.P. and Barbosa, M.A.}
}
@article {2268,
	title = {Bioactivity of immobilized EGF on self-assembled monolayers: Optimization of the immobilization process},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {94},
	year = {2010},
	note = {Cited By (since 1996): 7Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.32723PubMed ID: 20198690Language of Original Document: EnglishCorrespondence Address: Gon{\c c}alves, R.; INEB, Biomaterials Division, NEWTherapies Group, R. Campo Alegre, 823, Porto 4150-180, Portugal; email: raquelg@ineb.up.ptChemicals/CAS: epidermal growth factor, 62229-50-9; gold, 7440-57-5; Biocompatible Materials; Epidermal Growth Factor, 62229-50-9; Gold, 7440-57-5; Imidazoles; N,N-carbonyldiimidazole, 530-62-1; Polyethylene Glycols; Receptor, Epidermal Growth Factor, 2.7.10.1; Sulfhydryl CompoundsReferences: Singh, A., Harris, R.C., Autocrine, paracrine and juxtacrine signaling by EGFR ligands (2005) Cell Signal, 17, pp. 1183-1193;Luca, A., Carotenuto, A., Rachiglio, A., Gallo, M., Maiello, M.R., Aldinucci, D.L., Pinto, A., Normanno, N., The role of the EGFR signaling in tumor microenvironment (2008) J Cell Physiol, 214, pp. 559-567; 
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},
	month = {2010///},
	pages = {576 - 585},
	abstract = {Last trends in Biomaterials focus the mimic of cellular environments capable to control cellular responses. Epidermal growth factor (EGF) is a pleiotropic cytokine known to regulate cell proliferation, differentiation, and death. This study aims to optimize the immobilization of EGF on 11-mercapto-1-undecyl-tetra(ethylene)glycol (EG4) - self-assembled monolayers (SAMs) and to establish a new model surface to study EGF-mediated signaling. Gold substrates were modified with a monolayer of EG4 and N,N'- carbonyldiimidazole (CDI) was used to activate hydroxyl terminated groups of EG4-SAMs. EGF was then immobilized on activated EG4-SAMs at pH 7.4, 4{\textdegree}C, and 100 rpm. Different immobilization reaction times were tested as well as different CDI concentrations to optimize the reaction conditions and obtain a range of immobilized EGF concentrations on the surfaces. Surface characterization of EGF-SAMs was performed using radiolabeling, water contact angle measurements, X-ray photoelectron spectroscopy, and ELISA. Phosphorylation of EGFR on BT-20 breast cancer cell line by EGF-SAMs was tested by immunostaining. EGF was successfully immobilized on EG4-SAMs, at 4{\textdegree}C and pH 7.4 in a range of concentrations from 3.6 {\textpm} 0.8 to 17.6 {\textpm} 1.5 ng/cm                        2. The concentration of EGF increases with immobilization time and with the CDI concentration reaching the maximum for surfaces activated with 30 mg/mL of CDI after 48 h. The bioactivity of EGF-SAMs was confirmed by immunostaining of phospho-EGFR of BT-20 cells. This study described EGF immobilization on EG4-SAMs at different concentrations, which could be important surface models to study specific protein interactions at the molecular level evolving EGF-family of proteins. {\textcopyright} 2010 Wiley Periodicals, Inc. J.
},
	keywords = {Adsorption, Angle measurement, article, Biocompatible Materials, Biological materials, Breast cancer cells, cancer cell culture, Carbonyldiimidazole, Cell culture, Cell immobilization, Cell Line, Tumor, cell proliferation, Cellular environment, Cellular response, Concentration (process), Concentration of, Contact angle, controlled study, Cytokines, EGF, Electron energy levels, enzyme linked immunosorbent assay, Enzyme-Linked Immunosorbent Assay, epidermal growth factor, Epidermal growth factors, Ethylene, Glycols, gold, Gold substrates, human, human cell, Humans, Hydroxyl-terminated, Imidazoles, Immobilization process, Immobilization reaction, immunofluorescence, immunohistochemistry, Immunostaining, Molecular levels, Nanostructured materials, Nanostructured surface, Nanostructured surfaces, New model, Optimization, Phosphorylation, Photoelectron spectroscopy, Polyethylene Glycols, Protein adsorption, protein immobilization, protein interaction, protein phosphorylation, Proteins, Radiolabeling, Radioligand Assay, Reaction conditions, reaction optimization, Receptor, Epidermal Growth Factor, Sams, self assembled monolayer, Self assembled monolayers, Self-assembled monolayers, Sulfhydryl Compounds, Surface characterization, Surface functionalization, Surface models, Surface Properties, Water contact angle measurement, X ray photoelectron spectroscopy},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77953815323\&partnerID=40\&md5=7b54d717bbba475933dd86cc62659acc},
	author = {Gon{\c c}alves, R. and Martins, M.C.L. and Oliveira, M.J. and Almeida-Porada, G. and Barbosa, M.A.}
}
@article {2279,
	title = {The effect of immobilization of thrombin inhibitors onto self-assembled monolayers on the adsorption and activity of thrombin},
	journal = {BiomaterialsBiomaterials},
	volume = {31},
	year = {2010},
	note = {Cited By (since 1996): 7Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2010.01.097PubMed ID: 20153046Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal; email: cmartins@ineb.up.ptChemicals/CAS: thrombin, 9002-04-4; Albumins; Gold, 7440-57-5; Immobilized Proteins; Iodine Radioisotopes; Peptides; Solutions; Thrombin, 3.4.21.5References: Gorbet, M.B., Sefton, M.V., Biomaterial-associated thrombosis: roles of coagulation factors, complement, platelets and leukocytes (2004) Biomaterials, 25 (26), pp. 5681-5703;Ratner, B.D., Hoffman, A.F., Schoen, F.J., Lemons, J.L., (2004) Biomaterials science - an introduction to materials in medicine. 2nd ed., , Elsevier Academic Press, San Diego, CA, USA; 
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},
	month = {2010///},
	pages = {3772 - 3780},
	abstract = {Thrombus formation is the major problem associated with biomaterials for blood contact medical devices. The immobilization of inhibitors to thrombin, a serine protease that plays a central role on the coagulation system, on the surface of biomaterials should be a good strategy to avoid blood clotting and increase their hemocompatibility. The aim of this work is the design of a nanostructured surface with capacity to adsorb and inactivate thrombin. The pentapeptide sequence d-Phenylalanine-Proline-Arginine-Proline-Glycine (fPRPG), that was described as a thrombin inhibitor, was immobilized onto tetra(ethylene glycol) terminated self-assembled monolayers (EG4-SAMs). Surface containing different amounts of fPRPG were prepared using different concentrations of N,N'-Carbonyldiimidazole (CDI) during immobilization. The efficiency of fPRPG immobilization was followed using ellipsometry, contact angle measurements, Infrared reflection absorption spectroscopy (IRRAS) and X-ray photoelectron spectroscopy (XPS). Thrombin adsorption was quantified using radiolabelled thrombin and its activity in solution and after adsorption on the developed surfaces was assessed using a chromogenic assay. It was found that, although the immobilization of fPRPG on to EG4-SAMs does not increase its selectivity to thrombin, the activity of the adsorbed thrombin was inhibited in a peptide concentration dependent way. We concluded that SAMs with fPRPG immobilized in high amounts can be used as thrombin-inhibitor surfaces, which is a good step on the development of new surfaces for blood contact devices. {\textcopyright} 2010 Elsevier Ltd. All rights reserved.},
	keywords = {Absorption spectroscopy, Adsorption, adsorption kinetics, Albumins, Amino Acid Sequence, Amino acids, Angle measurement, article, Biomaterials, Blood, Blood clotting, Blood contact, Carbonyldiimidazole, Coagulation, Coagulation system, concentration (parameters), Concentration-dependent, Contact angle, D-phenylalanine, ellipsometry, Ethylene, Ethylene Glycol, ethylene glycol derivative, gold, Hemocompatibility, Humans, imidazole derivative, Immobilized Proteins, Infrared reflection absorption spectroscopy, infrared spectroscopy, Iodine Radioisotopes, isotope labeling, Medical Devices, monolayer culture, nanoanalysis, Nanostructured surface, peptide, Peptide immobilization, Peptides, phenylalanylprolylarginylprolylglycine, Phosphatases, priority journal, Protein adsorption, protein assembly, protein function, protein immobilization, quantitative study, Sams, Self assembled monolayers, Self-assembled monolayers, Serine protease, Solubility, Solutions, Spectroscopy, Fourier Transform Infrared, Surface functionalization, Surface Properties, Tetra, tetra(ethylene glycol), Thrombin, thrombin inhibitor, Thrombin inhibitors, Thrombus formation, unclassified drug, X ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77649271932\&partnerID=40\&md5=f7180daf23d326319cf6d8dbf0eac77c},
	author = {Freitas, S.C. and Barbosa, M.A. and Martins, M.C.L.}
}
@article {2255,
	title = {The stability of self-assembled monolayers with time and under biological conditions},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {94},
	year = {2010},
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},
	month = {2010///},
	pages = {833 - 843},
	abstract = {The stability of self-assembled monolayers (SAMs) of different functionalities (CH                        3
},
	keywords = {Animals, article, Binding energy, Biological conditions, Biological studies, Body fluids, Cattle, Cell culture, Culture Media, Ethanol, Female, Fetal bovine serum, In-cell, materials testing, measurement, molecular stability, Nitrogen chamber, nonhuman, Organic polymers, Oxidation, Oxidation-Reduction, Oxidized sulfur, Photodegradation, Photoelectron spectroscopy, Sams, self assembled monolayer, Self assembled monolayers, Self-assembled monolayers, Stability, Storage condition, Sulfhydryl Compounds, Sulfur, Surface Properties, Water, wettability, X ray photoelectron spectroscopy, XPS, XPS spectra},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77954806701\&partnerID=40\&md5=9c561e8b43c045cdeb8d80a42148c6ca},
	author = {Maciel, J. and Martins, M.C.L. and Barbosa, M.A.}
}
@article {2323,
	title = {The correlation between the adsorption of adhesive proteins and cell behaviour on hydroxyl-methyl mixed self-assembled monolayers},
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	year = {2009},
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Rodrigues, S.N., Gon{\c c}alves, I.C., Martins, M.C., Barbosa, M.A., Ratner, B.D., Fibrinogen adsorption, platelet adhesion and activation on mixed hydroxyl-/methyl-terminated self-assembled monolayers (2006) Biomaterials, 27, pp. 5357-5367; 
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},
	month = {2009///},
	pages = {307 - 316},
	abstract = {The objective of this study was to compare the biological effects of two key cell-adhesive proteins, fibronectin (FN) and vitronectin (VN), upon adsorption onto molecularly-designed model surfaces. Single-component and mixed self-assembled monolayers (SAMs) of alkanethiols on gold with OH and CH                        3 terminal groups were prepared at 100\%, 65\%, 36\% and 0\% of OH at the surface, to generate a range of surfaces with a simple chemistry and a wettability gradient. FN and VN were adsorbed under non-competitive (single-protein solutions) and competitive (multi-protein solutions) conditions, and compared at different levels: adsorbed amount (radiolabelling), elution, functional presentation of cell-binding domains (ELISA), and role in mediating cell adhesion (antibody-based assay). The observed trends were related to mesenchymal stem cell response in terms of adhesion and overall cell morphology. Under non-competitive conditions, adsorption of both proteins increased with surface hydrophobicity. The presence of competitive proteins significantly decreased the adsorbed amounts, although both proteins were still detected in all SAMs. Adsorption of FN followed a trend similar to that of non-competitive conditions, while adsorption of VN was higher on 100\%OH-SAMs. Concerning elution, retention of adsorbed VN was always higher than that of FN. For both proteins, functional presentation of cell-binding domains was more effective on the more hydrophilic 100\%OH-SAMs. This fact, coupled to the ability of this type of SAMs to selectively recruit and retain VN in the presence of competitive serum proteins, seems to correlate with the better cell response observed on these surfaces, as compared with hydrophobic 0\%OH(100\%CH
                        3)-SAMs. {\textcopyright} 2008 Elsevier Ltd. All rights reserved.
},
	keywords = {Adhesion, Adhesiveness, Adsorption, alkane, Animals, article, Biocompatible Materials, Biological Assay, bone marrow, Cattle, cell adhesion, Cell culture, Cell Movement, Cells, Cells, Cultured, cytology, cytoskeleton, Electric currents, Electron energy levels, enzyme linked immunosorbent assay, Fibronectin, Fibronectins, Focal adhesions, Functional groups, Functionalization, gold, human, human cell, Humans, hydrophilicity, hydrophobicity, Hydroxylation, isotope labeling, Mesenchymal stem cell, Mesenchymal Stem Cells, Microscopy, Confocal, Missile bases, Molecular interactions, monoclonal antibody, priority journal, Protein adsorption, protein analysis, protein binding, Protein Structure, Tertiary, Proteins, Self assembled monolayers, Self-assembled monolayers, stem cell, Stem cells, Surface Properties, thiol derivative, Vitronectin},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-55249093830\&partnerID=40\&md5=132fa4efe300c4f76764942bfe3bce30},
	author = {Barrias, C.C. and Martins, M.C.L. and Almeida-Porada, G. and Barbosa, M.A. and Granja, P.L.}
}
@article {2291,
	title = {Induction of notch signaling by immobilization of jagged-1 on self-assembled monolayers},
	journal = {BiomaterialsBiomaterials},
	volume = {30},
	year = {2009},
	note = {Cited By (since 1996): 6Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2009.09.010PubMed ID: 19783294Language of Original Document: EnglishCorrespondence Address: Gon{\c c}alves, R.M.; INEB, Biomaterials Division, NEWTherapies Group, R. Campo Alegre, 823, 4150-180 Porto, Portugal; email: raquelg@ineb.up.ptChemicals/CAS: Calcium-Binding Proteins; Gold, 7440-57-5; Immunoglobulin G; Intercellular Signaling Peptides and Proteins; Membrane Proteins; Receptors, Fc; Receptors, Notch; Recombinant Fusion Proteins; Serrate proteins, 134324-36-0References: Artavanis-Tsakonas, S., Rand, M.D., Lake, R.J., Notch signaling: cell fate control and signal integration in development (1999) Science, 284, pp. 770-776;Leong, K., Karsan, A., Recent insights in the role of notch signaling in tumorigenesis (2006) Blood, 107 (6), pp. 2223-2233; 
Chiba, S., Concise review: notch signaling in stem cell systems (2006) Stem Cells, 24, pp. 2437-2447; 
Lowell, S., Benchoua, A., Heavey, B., Smith, A.G., Notch promotes neural lineage entry by pluripotent embryonic stem cells (2006) PLoS Biol, 4 (5); 
Hellstr{\"o}m, M.P.L., Hofmann, J.J., Wallgard, E., Coultas, L., Lindblom, P., Alva, J., Dll4 signalling through notch1 regulates formation of tip cells during angiogenesis (2007) Nature, 15 (445), pp. 776-780; 
Hofmeister, C., Zhang, J., Knight, K.L., Le, P., Stiff, P.J., Ex vivo expansion of umbilical cord blood stem cells for transplantation: growing knowledge from the hematopoietic niche (2007) Bone Marrow Transplant, 39 (1), pp. 11-23; 
Hilton, M., Tu, X., Wu, X., Bai, S., Zhao, H., Kobayashi, T., F. Notch signaling maintains bone marrow mesenchymal progenitors by suppressing osteoblast differentiation (2008) Nat Med, 14 (3), pp. 306-314; 
Stylianou, S., Clarke, R.B., Brennan, K., Aberrant activation of notch signaling in human breast cancer (2006) Cancer Res, 66 (3), pp. 1517-1525; 
Demarest, R., Ratti, F., Capobianco, A.J., It{\textquoteright}s T-ALL about notch (2008) Oncogene, 27 (38), pp. 5082-5091; 
Fre, S., Huyghe, M., Mourikis, P., Robine, S., Louvard, D., Artavanis-Tsakonas, S., Notch signals control the fate of immature progenitor cells in the intestine (2005) Nature, 16 (435), pp. 964-968; 
Fischer, A., Gessler, M., Delta-notch-and then? Protein interactions and proposed modes of repression by Hes and Hey bHLH factors (2007) Nucleic Acids Res, 35 (14), pp. 4583-4596; 
Zweidler-McKay, P.A., He, Y., Xu, L., Rodriguez, C.G., Karnell, F.G., Carpenter, A.C., Notch signaling is a potent inducer of growth arrest and apoptosis in a wide range of B-cell malignancies (2005) Blood, 106 (12), pp. 3898-3906; 
Beckstead, B., Santosa, D.M., Giachelli, C.M., Mimicking cell-cell interactions at the biomaterial-cell interface for control of stem cell differentiation (2006) J Biomed Mater Res, 79 A, pp. 94-103; 
Varnum-Finney, B., Wu, L., Yu, M., Brashem-Stein, C., Staats, S., Flowers, D., Immobilization of Notch ligand, Delta-1, is required for induction of notch signaling (2000) J Cell Sci, 113 (23), pp. 4313-4318; 
Delaney, C., Varnum-Finney, B., Aoyama, K., Brashem-Stein, C., Bernstein, I.D., Dose-dependent effects of the notch ligand delta1 on ex vivo differentiation and in vivo marrow repopulating ability of cord blood cells (2005) Blood, 106, pp. 2693-2699; 
Lefort, N., Bennea, C., Leli{\`e}vrea, J.D., Dorivala, C., Balboa, M., Sakanoc, S., Short exposure to notch ligand delta-4 is sufficient to induce T-cell differentiation program and to increase the T cell potential of primary human CD34+ cells (2006) Exp Hematol, 34, pp. 1720-1729; 
Taqvi, S., Dixit, L., Krishnendu, R., Biomaterial-based notch signaling for the differentiation of hematopoietic stem cells into T cells (2006) J Biomed Mater Res, 79 A, pp. 689-697; 
Bernstein, I., Delaney, C., Dallas, M., Heimfeld, S., Varnum-Finney, B., Notch signaling in hematopoiesis: implication for improving stem cell transplantation (2008) Biol Blood Marrow Transplant, 14, pp. 94-99; 
De Smedt, M., Hoebeke, I., Reyvoet, K., Leclercq, G., Plum, J., Different thresholds of~Notch signaling bias human precursor cells toward B-, NK-, monocytic/dendritic-, or T-cell lineage in thymus microenvironment (2005) Blood, 106, pp. 3498-3506; 
Mrksich, M., What can surface chemistry do for cell biology? (2002) Curr Opin Chem Biol, 6, pp. 794-797; 
France, R., Short, R.D., Dawsonb, R.A., MacNeilb, S., Attachment of human keratinocytes to plasma copolymers of acrylic acid/octa-1,7-diene and allyl amine/octa-1,7-diene (1998) J Mater Chem, 81 (1), pp. 37-42; 
Neves, H., Weerkamp, F., Gomes, A.C., Naber, B., Gameiro, P., Becker, J.L., Effects of delta1 and jagged1 on early human hematopoiesis: correlation with expression of notch signaling-related genes in CD34+ Cells (2006) Stem Cells, 24, pp. 1328-1337; 
Sokolova, V., Epple, M., Inorganic nanoparticles as carriers of nucleic acids into cells (2008) Angewandte Chemie, 47, pp. 1382-1395; 
Yao, J., Duan, L., Fan, M., Yuan, J., Wu, X., Notch1 induces cell cycle arrest and apoptosis in human cervical cancer cells: involvement of nuclear factor kappa B inhibition (2007) Int J Gynecol Cancer, 17, pp. 502-510; 
Chadwick, N., Nostro, M.C., Baron, M., Mottram, R., Brady, G., Buckle, A., Notch signaling induces apoptosis in primary human CD34+ hematopoietic progenitor cells (2007) Stem Cells, 25, pp. 203-210; 
Love, J., Estroff, L.A., Kriebel, J.K., Nuzzo, R.G., Whitesides, G.M., Self-assembled monolayers of thiolates on metals as a form of nanotechnology (2005) Chem Rev, 105, pp. 1103-1169; 
Gehanno, V., Freitas, P.P., Veloso, A., Ferreira, J., Almeida, B., Sousa, J.B., Ion beam deposition of Mn-Ir spin valves (1999) IEEE Trans Magn, 35, pp. 4361-4367; 
Martins, M.C.L., Ratner, B., Barbosa, M.A., Protein adsorption on mixtures of hydroxyl- and methyl- terminated self-assembled monolyers (2003) J Biomed Mater Res, 67 (A), pp. 158-171; 
Martins, M.C.L., Curtins, S.A., Freitas, S.C., Salgueiro, P., Ratner, B.D., Barbosa, M.A., Molecularly designed surfaces for blood deheparinization using an immobilized heparin-binding peptide (2009) J Biomed Mater Res A, 88 (1), pp. 162-173; 
Barrias, C.C., Martins, M.C.L., Bidarra, S., S{\'a} Miranda, M.C., Barbosa, M.A., Adsorption of a therapeutic enzyme to self-assembled monolayers: effect of the surface chemistry and solution pH on the amount and activity of adsorbed enzyme (2005) Biomaterials, 26, pp. 2695-2704; 
Iodine-125. A guide to radioiodination techniques. In: techniques I-Agtr, ed.: Little Chalfort: Amersham Life Science 1993Horbett, T., Techniques for protein adsorption studies (1986) Techniques of biocompatibility tests, pp. 183-214. , DF W. (Ed), CRC Press Inc, Harcover; 
Ohishi, K., Varnum-Finney, B., Bernstein, I.D., Delta-1 enhances marrow and thymus repopulating ability of human CD34+ CD38- cord blood cells (2002) J Clin Invest, 110, pp. 1165-1174; 
Li, L., Chen, S., Zheng, J., Ratner, B.D., Jiang, S., Protein adsorption on oligo(ethylene glycol)-terminated alkanethiolate self-assembled monolayers: the molecular basis for nonfouling behavior (2005) J Phys Chem B, 109 (7), pp. 2934-2941; 
Tohda, S., Murata-Ohsawa, M., Sakano, S., Nara, N., Notch ligands, Delta-1 and Delta-4 supress the self-renewal capacity and long-term growth of two myeloblastic leukemia cell lines (2003) Int J Oncol, 22 (5), pp. 1073-1079; 
Tohda, S.K.H., Murakami, N., Sakano, S., Nara, N., Diverse effects of the Notch ligands Jagged1 and Delta1 on the growth and differentiation of primary acute myeloblastic leukemia cells (2005) Exp Hematol, 33, pp. 558-563; 
Aoyama, K., Delaney, C., Varnun-Finney, B., Kohn, A.D., Moon, R.T., Bernstein, I.D., The interaction of the Wnt and notch pathways modulates natural killer versus T cell differentiation (2007) Stem Cells, 25, pp. 2488-2497; 
Beckstead B, Tung JC, Liang KJ, Tavakkol Z, Usui ML, Olerud JE, et~al. Methods to promote notch signaling at the biomaterial interface and evaluation in a rafted organ culture model. J Biomed Mater Res A, in press. [Epub ahead of print]Semler, E., Dasgupta, A., Moghe, P.V., Cytomimetic engineering of hepatocyte morphogenesis and function by substrate-based presentation of acellular E-cadherin (2005) Tissue Eng, 11 (5-6), pp. 734-750; 
Zhao, Z., Matsui, H., Accurate immobilization of antibody-functionalized peptide nanotubes on protein-patterned arrays by optimizing their ligand-receptor interactions (2007) Small, 3 (8), pp. 1390-1393; 
Longo, G., Szleifer, Ligand-receptor interactions in tethered polymer layers (2005) Langmuir, 21, pp. 11342-11351; 
Gon{\c c}alves, I.C., Martins, M.C.L., Barbosa, M.A., Ratner, B.D., Protein adsorption and clotting time of pHEMA hydrogels modified with C18 ligands to adsorb albumin selectively and reversibly (2009) Biomaterials, 30 (29), pp. 5541-5551
},
	month = {2009///},
	pages = {6879 - 6887},
	abstract = {Notch signaling is a key mechanism during mammal development and stem cell regulation. This study aims to target and control Notch signaling by ligands immobilization using self-assembled monolayers (SAMs) as model surfaces. Non-fouling substrates were prepared by immersion of gold substrates in (1-Mercapto-11-undecyl)tetra(ethylene glycol) thiol solutions. These surfaces were activated with N,N'-carbonyldiimidazole (CDI) at different concentrations (0, 0.03, 0.3, 3 and 30 mg/ml) and an anti-human IgG, Fc specific fragment antibody (Ab) was covalently bound to EG4-SAMs to guarantee the correct exposure of the Notch ligand Jagged-1/Fc chimera (Jag-1). The presence of Ab and Jag-1 was confirmed by radiolabeling, X-ray photoelectron spectroscopy (XPS), ellipsometry and ELISA. The biological activity of Jag-1-Ab-SAMs was assessed by real-time PCR for Hes-1 family gene expression, a Notch pathway target gene, in HL-60 cell line. Results have shown an increase of the amount of immobilized Ab with increasing surface activator concentrations. Jag-1 concentration also increases with Ab concentration. Interestingly, a higher Jagged-1 exposure and fold increase in Hes-1 expression were obtained for surfaces activated with the lowest concentration of CDI (0.03 mg/ml). These results illustrate the great importance of ligands orientation and exposure, when compared with density. This investigation brings new insights into Notch signaling mechanisms. In particular, Jag-1-Ab-SAMs have shown to be adequate model surfaces to study Notch pathway activation and may provide a basis to develop new interfaces in biomaterials to control Notch mechanism in different cell systems. {\textcopyright} 2009 Elsevier Ltd.},
	keywords = {Activator concentration, Adequate models, Adsorption, Animals, article, Bioactivity, Biological activities, Biological materials, biomaterial, Calcium-Binding Proteins, Carbonyldiimidazole, Cell culture, Cell Line, Cell membranes, cell strain HL 60, Cell system, Chemical activation, Concentration (process), Concentration of, controlled study, Covalently bound, Ethylene, Ethylene Glycol, gene expression, gold, Gold substrates, HL-60 cell line, human, human cell, Human IgG, Humans, Immunoassay, immunoglobulin Fc fragment, Immunoglobulin G, immunoglobulin G antibody, Intercellular Signaling Peptides and Proteins, Jagged1, Ligands, Mammalia, Membrane Proteins, Model surface, Molecular Structure, Nanostructured materials, Nanostructured surfaces, Nonfouling, Notch receptor, Notch signaling, Photoelectron spectroscopy, priority journal, Protein adsorption, protein immobilization, Radiolabeling, Real-time PCR, Receptors, Fc, Receptors, Notch, Recombinant Fusion Proteins, Sams, self assembled monolayer, Self assembled monolayers, Self-assembled monolayers, signal transduction, Signaling, stem cell, Surface Properties, Target genes, Tetra, transcription factor HES 1, X ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-70350188310\&partnerID=40\&md5=6c55d29cf8ae55288f3e87880171ec70},
	author = {Gon{\c c}alves, R.M. and Martins, M.C.L. and Almeida-Porada, G. and Barbosa, M.A.}
}
@article {2325,
	title = {Molecularly designed surfaces for blood deheparinization using an immobilized heparin-binding peptide},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {88},
	year = {2009},
	note = {Cited By (since 1996): 12Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.31849PubMed ID: 18286636Language of Original Document: EnglishCorrespondence Address: Martins, M. C. L.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomaterials, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180, Porto, Portugal; email: cmartins@ineb.up.ptChemicals/CAS: carbonyldiimidazole, 530-62-1; heparin, 37187-54-5, 8057-48-5, 8065-01-8, 9005-48-5; imidazole, 1467-16-9, 288-32-4; leucine, 61-90-5, 7005-03-0; lysine, 56-87-1, 6899-06-5, 70-54-2; tetraethylene glycol, 112-60-7; Ethylene Glycol, 107-21-1; Heparin, 9005-49-6; Leucine, 61-90-5; Lysine, 56-87-1; PeptidesReferences: Dailey J. Blood. Ipswich, MA, USA: Medical Consulting Group; 1998Section, V., Chronic intermittent haemodialysis and prevention of clotting in the extracorporal system (2002) Nephrol Dialysis Transplant, 17, pp. 63-71;Zhang, Y.H., Singh, V.K., Yang, V.C., Novel approach for optimizing the capacity and efficacy of a protamine filter for clinical extracorporeal heparin removal (1998) Asaio J, 44, pp. M368-M373; 
Tao, W., Deyo, D.J., Brunston, R.L., Vertrees, R.A., Zwischenberger, J.B., Extracorporeal heparin adsorption following cardiopulmonary bypass with a heparin removal device - An alternative to protamine (1998) Critical Care Med, 26, pp. 1096-1102; 
Ameer, G.A., Barabino, G., Sasisekharan, R., Harmon, W., Cooney, C.L., Langer, R., Ex vivo evaluation of a Taylor-Couette flow, immobilized heparinase I device for clinical application (1999) Proc Natl Acad Sci USA, 96, pp. 2350-2355; 
Ostuni, E., Yan, L., Whitesides, G.M., The interaction of proteins and cells with self-assembled monolayers of alkanethiolates on gold and silver (1999) Colloids Surf B-Biointerfaces, 15, pp. 3-30; 
Mrksich, M., Whitesides, G.M., Using self-assembled monolayers that present oligo(ethylene glycol) groups to control the interactions of proteins with surfaces. Poly(Ethylene Glycol) (1997) ACS Symposium Series, 680, pp. 361-373; 
Cardin, A.D., Weintraub, H.J.R., Molecular modeling of proteinglycosaminoglycan interactions (1989) Arteriosclerosis, 9, pp. 21-32; 
Kricheldorf, H.R., (1987) α-Amino Acid N-Carboxyanhydrides and Related Heterocycles, , New York: Springer Verlag;; 
Martins, M.C.L., Ratner, B.D., Barbosa, M.A., Protein adsorption on mixtures of hydroxyl- and methylterminated alkanethiols self-assembled monolayers (2003) J Biomed Mater Res A, 67, pp. 158-171; 
Lee, H.J., Nedelkov, D., Corn, R.M., Surface plasmon resonance imaging measurements of antibody arrays for the multiplexed detection of low molecular weight protein biomarkers (2006) Anal Chem, 78, pp. 6504-6510; 
Roeges, N.P.G., (1994) A Guide to the Complete Interpretation of Infrared Spectra of Organic Structures, , England: Wiley;; 
Li, L.Y., Chen, S.F., Zheng, J., Ratner, B.D., Jiang, S.Y., Protein adsorption on oligo(ethylene glycol)-terminated alkanethiolate self-assembled monolayers: The molecular basis for non-fouling behavior (2005) J Phys Chem B, 109, pp. 2934-2941; 
Beamson, G., High, B.D., (1992) Resolution XPS of Organic Polymers, , Chichester: Wiley;; 
Sousa, S.R., Moradas, F.P., Saramago, B., Viseu, M.L., Barbosa, M.A., Human serum albumin adsorption on TiO2 from single protein solutions and from plasma (2004) Langmuir, 20, pp. 9745-9754; 
Socrates, G., (2001) Infrared and Raman Characteristic Group Frequencies: Tables and Charts, , Chichester: Wiley;; 
Capila, I., Linhardt, R.J., Heparin - Protein interactions (2002) Angewandte Chemie-Int Ed, 41, pp. 391-112; 
Snell, C.R.F.G., Kinetics and thermodynamics of the alpha Helix - β Transconformation of poly(L-lysine) and L-leucine copolymers. A compensation phenomenon (1973) Biochemistry, 12, pp. 1017-1025; 
Hearn, M.T.W., 1,1'-Carbonyldiimidazole-mediated immobilization of enzymes and affinity ligands (1987) Methods Enzymol, 135, pp. 102-117; 
Stollner, D., Scheller, F.W., Warsinke, A., Activation of cellulose membranes with 1,1'-carbonyldiimidazole or 1-cyano-4-dimethylaminopyridinium tetrafluoroborate as a basis for the development of immunosensors (2002) Anal Biochem, 304, pp. 157-165
},
	month = {2009///},
	pages = {162 - 173},
	abstract = {Systemic heparinization, used during haemodialysis to prevent blood clotting on the extracorporeal circuit, leads to a high incidence of hemorrhagic complications. The adverse reactions associated with heparin neutralization using protamine sulphate justify the development of an alternative system for blood deheparinization. The main objective of this work is to design nanostructured surfaces with the capacity to bind heparin from blood in a selective way. A heparin-binding polypeptide, composed of L-lysine and L-leucine (pKL), was synthesized and immobilized, in different concentrations, onto self-assembled monolayers (SAMs) terminated with tetra(ethylene-glycol) (EG4 SAMs). Immobilization was performed using a fixed concentration of pKL after surface activation to different degrees using a range of CDI (N,N'-carbonyldiimidazole) concentrations. Results demonstrated that the presence of pKL increases heparin adsorption to EG4-SAMs, independently of the pKL concentration and the way of immobilization (adsorption or covalent bound). Selectivity towards heparin was successfully achieved on SAMs with low concentrations of immobilized pKL (9-17\% of pKL). Surfaces were characterized using ellipsometry, contact angle measurements, Fourier transform infrared reflection absorption spectroscopy (IRAS), atomic force microscopy, and X-ray photoelectron spectroscopy. Heparin adsorption was assessed using IRAS and N-sulphonate-                        35S-heparin. Therefore, this study could give a good contribution for the design of blood deheparinization devices. {\textcopyright} 2008 Wiley Periodicals, Inc.
},
	keywords = {Absorption spectroscopy, Adsorption, Alternative systems, Amines, Amino acids, Angle measurement, article, Atomic force microscopy, Atomic forces, Atomic spectroscopy, Binding peptides, Blood, Blood clotting, Carbonyl diimidazole, Carbonyldiimidazole, Contact angle, deheparinization, device, Dialysis, Electron energy levels, ellipsometry, Ethylene, Ethylene Glycol, Fourier Transform Infrared, Fourier transforms, Glycols, Haemodialysis, heparin, heparin binding protein, Heparinization, High incidences, Humans, imidazole, immobilization, infrared spectroscopy, leucine, Low concentrations, lysine, Methods, Missile bases, Monolayers, nanomaterial, Nanostructured surfaces, Nanostructures, Peptide immobilization, Peptides, Photoelectron spectroscopy, Polysaccharides, Protein adsorption, protein binding, Renal Dialysis, Self assembled monolayers, Self-assembled monolayers, Sulphate, Surface activations, Surface functionalization, Surface Properties, surface property, tetraethylene glycol, unclassified drug, X ray photoelectron spectroscopy, X-ray photoelectron spectroscopies},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-57449118932\&partnerID=40\&md5=8f442ccbde0273f4ed4e04024a75fd37},
	author = {Martins, M.C.L. and Curtin, S.A. and Freitas, S.C. and Salgueiro, P. and Ratner, B.D. and Barbosa, M.A.}
}
@article {2309,
	title = {Selective protein adsorption modulates platelet adhesion and activation to oligo(ethylene glycol)-terminated self-assembled monolayers with C18 ligands},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {89},
	year = {2009},
	note = {Cited By (since 1996): 11Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.32011PubMed ID: 18442116Language of Original Document: EnglishCorrespondence Address: Gon{\c c}alves, I. C.; INEB-Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Universidade do Porto, Run do Campo Alegre, 823, 4150-180 Porto, Portugal; email: icastro@ineb.up.ptChemicals/CAS: fibrinogen, 9001-32-5; glutaraldehyde, 111-30-8, 37245-61-7; human serum albumin, 9048-49-1; Carbon, 7440-44-0; Ethylene Glycol, 107-21-1; Ligands; Serum AlbuminReferences: Nath, N., Hyun, J., Ma, H., Chilkoti, A., Surface engineering strategies for control of protein and cell interactions (2004) Surf Sci, 570, pp. 98-110;Mao, C., Qiu, Y.Z., Sang, H.B., Mei, H., Zhu, A.P., Shen, J., Lin, S.C., Various approaches to modify biomaterial surfaces for improving hemocompatibility (2004) Adv Colloid Interface Sci, 110, pp. 5-17; 
Gorbet, M.B., Sefton, M.V., Biomaterial-associated thrombosis: Roles of coagulation factors, complement, platelets and leukocytes (2004) Biomaterials, 25, pp. 5681-5703; 
Kottkemarchant, K., Anderson, J.M., Umemura, Y., Marchant, R.E., Effect of albumin coating on the in vitro blood compatibility of dacron arterial prostheses (1989) Biomaterials, 10, pp. 147-155; 
Munro, M.S., Quattrone, A.J., Ellsworth, S.R., Kulkarni, P., Eberhart, R.C., Alkyl substituted polymers with enhanced albumin affinity (1981) Trans Am Soc Artif Intern Organs, 27, pp. 499-503; 
Eberhart, R.C., Munro, M.S., Williams, G.B., Kulkarni, P.V., Shannon, W.A., Brink, B.E., Fry, W.J., Albumin adsorption and retention on C-18-alkyl-derivatized polyurethane vascular grafts (1987) Artif Organs, 11, pp. 375-382; 
Frautschi, J.R., Munro, M.S., Lloyd, D.R., Eberhart, R.C., Alkyl derivatized cellulose-acetate membranes with enhanced albumin affinity (1983) Trans Am Soc Artif Intern Organs, 29, pp. 242-244; 
Pitt WG, Cooper SL. Albumin adsorption on alkyl chain derivatized polyurethanes. I. The effect of C-18 alkylation. T Biomed Mater Res 1988;22:359-382Johnston, E., Ratner, B.D., Protein Adsorption: Friend or Foe? (1998) Immobilized biomolecules in analysis: A practical approach, pp. 79-94. , Cass T, Ligler FS, editors, Oxford: Oxford University Press;; 
Ji, J., Feng, L.X., Barbosa, M.A., Stearyl poly(ethylene oxide) grafted surfaces for preferential adsorption of albumin (2001) Biomaterials, 22, pp. 3015-3023; 
Martins, M.C.L., Naeemi, E., Ratner, B.D., Barbosa, M.A., Albumin adsorption on cibacron blue F3G-A immobilized onto oligo (ethylene glycol)-terminated self-assembled monolayers (2003) J Mater Sci Mater Med, 14, pp. 945-954; 
Sigal, G.B., Mrksich, M., Whitesides, G.M., Effect of surface wettability on the adsorption of proteins and detergents (1998) J Am Chem Soc, 120, pp. 3464-3473; 
Palegrosdemange, C., Simon, E.S., Prime, K.L., Whitesides, G.M., Formation of self-assembled monolayers by chemisorption of derivatives of oligo(ethylene glycol) of structure Hs(Ch2)11 (Och2ch2)meta-Oh on gold (1991) J Am Chem Soc, 113, pp. 12-20; 
Goncalves, I.C., Martins, M.C.L., Barbosa, M.A., Ratner, B.D., Protein adsorption on 18-alkyl chains immobilized on hydroxyl-ter- minated self-assembled monolayers (2005) Biomaterials, 26, pp. 3891-3899; 
Martins MCL, Ratner BD, Barbosa MA. Protein adsorption on mixtures of hydroxyl- and methylterminated alkanethiols self-assembled monolavers. I Biomed Mater Res 2003;67A: 158-171Owens, D.K., Wendt, R.C., Estimation of surface free energy of polymers (1969) J Appl Polym Sci, 13, pp. 1741-1747; 
Sousa, S.R., Moradas Ferreira, P., Saramago, B., Viseu Melo, L., Barbosa, M.A., Human serum albumin adsorption on TiO 2 from single protein solutions and from plasma (2004) Langmuir, 20, pp. 9745-9754; 
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},
	month = {2009///},
	pages = {642 - 653},
	abstract = {This study focuses on the selective binding of albumin to a nanostructured surfaces to inhibit other blood proteins from adsorbing thereby reducing platelet adhesion and activation. Tetra (ethylene-glycol)-terminated self- assembled monolayers (EG4 SAMs) with different percentages of CI 8 ligands on the surface were characterized by contact angle measurements, X-ray photoelectron microscopy, infrared reflection-absorption spectroscopy, and ellipsometry. A specific surface (2.5\% C18 SAM) was found to be selective for human serum albumin (HSA) in the presence of both albumin and fibrinogen (HFG). The importance of this concentration of C18 ligands was stressed in reversibility studies since that surface exchanged almost all the preadsorbed HSA by HSA in solution, but not by HFG. The effect of protein adsorption in the subsequent adhesion and activation of platelets was studied by pre-immersing the surfaces in albumin and plasma before contact with platelets. Scanning electron microscopy and glutaraldehyde induced fluorescence technique images showed that as surfaces got more hydrophobic due to the immobilization of C18 ligands, the number of adherent platelets increased and their morphology changed from round to fully spread. Pre-immersion in HSA led to an 80{\textdegree}/o decrease in platelet adhesion and reduction of activation. Pre-immersion in 1\% plasma was only relevant in 2.5\% CI 8 SAMs since this was the only surface that demonstrated less adhesion of platelets comparing with buffer pre-immersion. However, they still adsorb more platelets then when HSA was preadsorbed. This was confirmed in competition studies between HSA and plasma that suggested that other plasma proteins were also adsorbing to this surface. {\textcopyright} 2008 Wiley Periodicals, Inc.},
	keywords = {Absorption spectroscopy, Acoustic microscopes, Adhesion, Adsorption, Albumin, Aldehydes, Angle measurement, article, Biological materials, Biomaterials, Blood Platelets, Blood protein, Blood substitutes, Carbon, Cell Shape, chemical composition, Concentration of, Contact angle, controlled study, Ethylene, Ethylene Glycol, ethylene glycol derivative, fibrinogen, Fluorescence technique, glutaraldehyde, gold nanoparticle, human, human serum albumin, Human serum albumins, Humans, hydrophobicity, Infrared reflection absorption spectroscopy, infrared spectroscopy, ligand, Ligands, Nanostructured surface, normal human, Oligo(ethylene glycol), Photoelectron spectroscopy, plasma, Plasma diagnostics, Plasma protein, Plasmas, Platelet adhesion, Platelet Adhesiveness, Platelets, Protein adsorption, protein binding, Proteins, Sams, Scanning electron microscopy, Selective binding, Selective protein adsorption, self assembled monolayer, Self assembled monolayers, Self-assembled monolayers, Serum Albumin, Specific surface, Spectrophotometry, Infrared, Surface Properties, surface property, thrombocyte activation, thrombocyte adhesion, thrombocyte shape, X ray photoelectron spectroscopy, X-ray photoelectron microscopy},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-66249128976\&partnerID=40\&md5=0be21ad44fe5cf556598975ea1655bed},
	author = {Gon{\c c}alves, I.C. and Martins, M.C.L. and Barbosa, M.A. and Naeemi, E. and Ratner, B.D.}
}
