



@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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Lahann, J., Pl{\"u}ster, W., Klee, D., Gattner, H.G., H{\"o}cker, H., Immobilization of the thrombin inhibitor r-hirudin conserving its biological activity (2001) J Mater Sci Mater Med, 12 (9), pp. 807-810; 
Phaneuf, M.D., Berceli, S.A., Bide, M.J., Quist, W.C., LoGerfo, F.W., Covalent linkage of recombinant hirudin to poly(ethylene terephthalate) (Dacron): creation of a novel antithrombin surface (1997) Biomaterials, 18 (10), pp. 755-765; 
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Martins, M.C.L., Curtin, 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; 
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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 (11), pp. 945-954; 
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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 {2272,
	title = {Receptor-mediated gene delivery using PAMAM dendrimers conjugated with peptides recognized by mesenchymal stem cells},
	journal = {Molecular PharmaceuticsMol. Pharm.},
	volume = {7},
	year = {2010},
	note = {Cited By (since 1996): 17Export Date: 21 November 2012Source: Scopusdoi: 10.1021/mp9002877PubMed ID: 20230026Language of Original Document: EnglishCorrespondence Address: Balian, G.; Orthopaedic Research Laboratories, Department of Orthopaedics and Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, VA 22908, United States; email: lenat@uma.ptChemicals/CAS: Dendrimers; Green Fluorescent Proteins, 147336-22-9; PAMAM Starburst; Peptides; enhanced green fluorescent proteinReferences: V{\"a}{\"a}n{\"a}nen, H.K., Mesenchymal stem cells (2005) Ann. Med., 37, pp. 469-479;Caplan, A.I., Adult mesenchymal stem cells for tissue engineering versus regenerative medicine (2007) J. Cell Physiol., 213, pp. 341-347; 
Kay, M.A., Glorioso, J.C., Naldini, L., Viral vectors for gene therapy: The art of turning infectious agents into vehicles of therapeutics (2001) Nat. Med., 7, pp. 33-40; 
Mastrobattista, E., Bravo, S.A., Van Der Aa, M., Crommelin, D.J.A., Nonviral gene delivery systems: From simple transfection agents to artificial viruses (2005) Drug Discovery Today: Technol., 2, pp. 103-109; 
Merdan, T., Kopecek, J., Kissel, T., Prospects for cationic polymers in gene and oligonucleotide therapy against cancer (2002) Adv. Drug Delivery Rev., 54, pp. 715-758; 
Hamm, A., Krott, N., Breibach, I., Blindt, R., Bosserhoff, A.K., Efficient transfection method for primary cells (2002) Tissue Eng., 8, pp. 235-245; 
McMahon, J.M., Conroy, S., Lyons, M., Greiser, U., O{\textquoteright}Shea, C., Strappe, P., Howard, L., O{\textquoteright}Brien, T., Gene transfer into rat mesenchymal stem cells: A comparative study of viral and nonviral vectors (2006) Stem Cells Dev., 15, pp. 87-96; 
Svenson, S., Tomalia, D.A., Dendrimers in biomedical applications-reflections on the field (2005) Adv. Drug Delivery Rev., 57, pp. 2106-2129; 
Duf-s, C., Uchegbu, I.F., Schatzlein, A.G., Dendrimers in gene delivery (2005) Adv. Drug Delivery Rev., 57, pp. 2177-2202; 
Guillot, M., Eisler, S., Diederich, F., Dendritic vectors for gene transfection (2007) New J. Chem., 31, pp. 1111-1127; 
Smith, D.K., Dendrimers and the double helix-from DNA binding towards gene therapy (2008) Curr. Top. Med. Chem., 8, pp. 1187-1203; 
Kukowska-Latallo, J.F., Bielinska, A.U., Johnson, J., Spindler, R., Tomalia, D.A., Baker Jr., J.R., Efficient transfer of genetic material into mammalian cells using Starburst polyamidoamine dendrimers (1996) Proc. Natl. Acad. Sci. U.S.A., 93, pp. 4897-4902; 
Santos, J.L., Oramas, E., P{\^e}go, A.P., Granja, P.L., Tom{\'a}s, H., Osteogenic differentiation of mesenchymal stem cells using PAMAM dendrimers as gene delivery vectors (2009) J. Controlled Release, 134, pp. 141-148; 
Balian, G., (2008), Bone Targeting Peptides. In United States Patent 7,323,542, issued January 29Snyder, S.L., Sobocinski, P.Z., An improved 2,4,6-trinitrobenzenesulfonic acid method for the determination of amines (1975) Anal. Biochem., 64, pp. 284-288; 
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Perrot, S., Dutertre-Catella, H., Martin, C., Rat, P., Warnet, J.M., Resazurin metabolism assay is a new sensitive alternative test in isolated pig cornea (2003) Toxicol. Sci., 72, pp. 122-129; 
Wood, K.C., Little, S.R., Langer, R., Hammond, P.T., A family of hierarchically self-assembling linear-dendritic hybrid polymers for highly efficient targeted gene delivery (2005) Angew. Chem., Int. Ed., 44, pp. 6704-6708; 
Dan Luo, K.H., Belcheva, N., Han, E., Mark Saltzman, W., Poly(ethylene glycol)-conjugated PAMAM dendrimer for biocompatible, high-efficiency dna delivery (2002) Macromolecules, 35, pp. 3456-3462; 
Schaffer, D.V., Lauffenburger, D.A., Optimization of cell surface binding enhances efficiency and specificity of molecular conjugate gene delivery (1998) J. Biol. Chem., 273, pp. 28004-28009; 
Santos, J.L., Oliveira, H., Pandita, D., P{\^e}go, A.P., Granja, P.L., Tom{\'a}s, H., Functionalization of poly(amidoamine) dendrimers with hydrophobic chains for improved gene delivery in mesenchymal stem cells (2010) J. Controlled Release, , doi: 10.1016/j.jconrel.2010.01.034
},
	month = {2010///},
	pages = {763 - 774},
	abstract = {As mesenchymal stem cells (MSCs) can differentiate into multiple cell types, the delivery of exogenous genes to this type of cell can be an important tool in tissue regeneration and engineering. However transfection of MSCs using nonviral gene delivery vectors is difficult, the development of more efficient and safe DNA vehicles being necessary. Moreover, specific transfection of MSCs may be required to avoid unwanted side effects in other tissues. In this study, a novel family of gene delivery vectors based on poly(amidoamine) (PAMAM) dendrimers functionalized with peptides displaying high affinity toward MSCs was prepared. The vectors were characterized with respect to their ability to neutralize, bind and compact plasmid DNA (pDNA). The complexes formed between the vectors and pDNA were analyzed concerning their size, -potential, capacity of being internalized by cells and transfection efficiency. These new vectors exhibited low cytotoxicity, receptor-mediated gene delivery into MSCs and transfection efficiencies superior to those presented by native dendrimers and by partially degraded dendrimers. {\textcopyright} 2010 American Chemical Society.},
	keywords = {animal cell, animal experiment, animal tissue, Animals, article, asparaginylserylmethionylisoleucylalanylhistidylasparaginyllysylthreonylarginylmethionylhistidylglycylglycylglycylserylcysteine, Cell recognition, cell survival, Cells, Cultured, controlled study, Cytotoxicity, dendrimer, Dendrimers, DNA, DNA binding, Electrophoresis, Agar Gel, flow cytometry, Gene delivery, gene targeting, Gene Transfer Techniques, gene vector, genetic transfection, Genetic Vectors, Green Fluorescent Proteins, male, Mesenchymal stem cell, Mesenchymal Stem Cells, Models, Theoretical, multigene family, nonhuman, PAMAM dendrimers, peptide, Peptides, plasmid DNA, polyamidoamine, priority journal, rat, Rats, Rats, Wistar, serylglycylhistidylglutaminylleucylleucylleucylasparaginyllysylmethionylprolylasparaginylglycylglycylglycylserylcysteine, unclassified drug, Zeta potential},
	isbn = {15438384 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77953253240\&partnerID=40\&md5=e06048334c689e2faa61e7b6b8ad9bf1},
	author = {Santos, J.L. and Pandita, D. and Rodrigues, J. and P{\^e}go, A.P. and Granja, P.L. and Balian, G. and Tom{\'a}s, H.}
}
