



@article {3273,
	title = {Characterization of hLF1-11 immobilization onto chitosan ultrathin films, and its effects on antimicrobial activity},
	journal = {Acta Biomaterialia},
	volume = {10},
	year = {2014},
	note = {Cited By (since 1996):1Export Date: 21 November 2014},
	month = {2014},
	pages = {3513 - 3521},
	abstract = {hLF1-11 (GRRRRSVQWCA) is an antimicrobial peptide (AMP) with high activity against methicillin-resistant Staphylococcus aureus (MRSA), the most prevalent species in implant-associated infection. In this work, the effect of the surface immobilization on hLF1-11 antimicrobial activity was studied. Immobilization was performed onto chitosan thin films as a model for an implant coating due to its reported osteogenic and antibacterial properties. Chitosan thin films were produced by spin-coating on gold surfaces. hLF1-11 was immobilized onto these films by its C-terminal cysteine in an orientation that exposes the antimicrobial activity-related arginine-rich portion of the peptide. Two levels of exposure (with and without a polyethylene glycol (PEG) spacer) were analyzed. Covalent immobilization was further compared with the AMP physical adsorption onto chitosan films. Surfaces were characterized using ellipsometry, contact angle measurements, atomic force microscopy, infrared and X-ray photoelectron spectroscopies and using a fluorimetric assay for hLF1-11 quantification. Surface antimicrobial activity was assessed through surface adhesion and viability assays using an MRSA (S. aureus ATCC 33591). The incorporation of hLF1-11 increased significantly bacterial adhesion to chitosan films. However, the presence of hLF1-11, namely when immobilized through a PEG spacer, decreased the viability of adherent bacteria with regard to the control surface. These results demonstrated that hLF1-11 after covalent immobilization by its cysteine can maintain activity, particularly if a spacer is applied. However, further studies, exploring the opposite orientation or the same C-terminal orientation, but non-cysteine related, can help to clarify the potential of the hLF1-11 immobilization strategy. {\textcopyright} 2014 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.},
	keywords = {Antimicrobial peptides (AMP), Bacterial adhesion, chitosan, Surface characterization, Surface immobilization},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84903724424\&partnerID=40\&md5=e8009cd480b49c37a991753cd145cf34},
	author = {Costa, F. and Maia, S. and Gomes, J. and Gomes, P. and Martins, M.C.L.}
}
@article {3296,
	title = {Hydrogel depots for local co-delivery of osteoinductive peptides and mesenchymal stem cells},
	journal = {Journal of Controlled Release},
	volume = {189},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {158 - 168},
	abstract = {The outcome of cell-based therapies can benefit from carefully designed cell carriers. A multifunctional injectable vehicle for the co-delivery of human mesenchymal stem cells (hMSCs) and osteoinductive peptides is proposed, to specifically direct hMSCs osteogenic differentiation. The osteogenic growth peptide (OGP) inspired the design of two peptides, where the bioactive portion of OGP was flanked by a protease-sensitive linker, or its scrambled sequence, to provide faster and slower release rates, respectively. Peptides were fully characterized and chemically grafted to alginate. Both OGP analogs released bioactive fragments in vitro, at different kinetics, which stimulated hMSCs proliferation and osteogenesis. hMSCs-laden OGP-alginate hydrogels were tested at an ectopic site in a xenograft mouse model. After 4 weeks, OGP-alginate hydrogels were more degraded and colonized by vascularized connective tissue than the control (without OGP). hMSCs were able to proliferate, migrate outward the hydrogels, produce endogenous extracellular matrix and mineralize it. Moreover, OGP-groups stimulated hMSCs osteogenesis, as compared with the control. Overall, the ability of the proposed platform to direct the fate of transplanted hMSCs in loco was demonstrated, and OGP-releasing hydrogels emerged as a potentially useful system to promote bone regeneration. {\textcopyright} 2014 Elsevier B.V.},
	keywords = {Bone Regeneration, Co-delivery systems, Guided differentiation, Injectable alginate hydrogels, Mesenchymal Stem Cells, Osteoinductive peptides},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84904318888\&partnerID=40\&md5=5f671d3584c3b7fc785ffaf40c2f0b1d},
	author = {Maia, F.R. and Barbosa, M. and Gomes, D.B. and Vale, N. and Gomes, P. and Granja, P.L. and Barrias, C.C.}
}
@article {3285,
	title = {Selective albumin-binding surfaces modified with a thrombin-inhibiting peptide},
	journal = {Acta Biomaterialia},
	volume = {10},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {1227 - 1237},
	abstract = {Blood-contacting medical devices have been associated with severe clinical complications, such as thrombus formation, triggered by the activation of the coagulation cascade due to the adsorption of certain plasma proteins on the surface of biomaterials. Hence, the coating of such surfaces with antithrombotic agents has been used to increase biomaterial haemocompatibility. Biomaterial-induced clotting may also be decreased by albumin adsorption from blood plasma in a selective and reversible way, since this protein is not involved in the coagulation cascade. In this context, this paper reports that the immobilization of the thrombin inhibitor D-Phe-Pro-D-Arg-D-Thr-CONH 2 (fPrt) onto nanostructured surfaces induces selective and reversible adsorption of albumin, delaying the clotting time when compared to peptide-free surfaces. fPrt, synthesized with two glycine residues attached to the N-terminus (GGfPrt), was covalently immobilized onto self-assembled monolayers (SAMs) having different ratios of carboxylate-hexa(ethylene glycol)- and tri(ethylene glycol)-terminated thiols (EG6-COOH/EG3) that were specifically designed to control GGfPrt orientation, exposure and density at the molecular level. In solution, GGfPrt was able to inactivate the enzymatic activity of thrombin and to delay plasma clotting time in a concentration-dependent way. After surface immobilization, and independently of its concentration, GGfPrt lost its selectivity to thrombin and its capacity to inhibit thrombin enzymatic activity against the chromogenic substrate n-p-tosyl-Gly-Pro-Arg-p-nitroanilide. Nevertheless, surfaces with low concentrations of GGfPrt could delay the capacity of adsorbed thrombin to cleave fibrinogen. In contrast, GGfPrt immobilized in high concentrations was found to induce the procoagulant activity of the adsorbed thrombin. However, all surfaces containing GGfPrt have a plasma clotting time similar to the negative control (empty polystyrene wells), showing resistance to coagulation, which is explained by its capacity to adsorb albumin in a selective and reversible way. This work opens new perspectives to the improvement of the haemocompatibility of blood-contacting medical devices. {\textcopyright} 2013 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.},
	keywords = {Albumin, Blood compatibility, Clotting, Surface modification, Thrombin},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84895067841\&partnerID=40\&md5=8486186625f8f4f1cbc538bb3e34dd82},
	author = {Freitas, S.C. and Maia, S. and Figueiredo, A.C. and Gomes, P. and Pereira, P.J.B. and Barbosa, M.A. and Martins, M.C.L.}
}
@article {2212,
	title = {Synthesis of an O-alkynyl-chitosan and its chemoselective conjugation with a PEG-like amino-azide through click chemistry},
	journal = {Carbohydrate PolymersCarbohydr Polym},
	volume = {87},
	year = {2012},
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},
	month = {2012///},
	pages = {240 - 249},
	abstract = {N-Phthaloyl-chitosan O-prop-2-ynyl carbamate was prepared as a biopolymer amenable to undergo chemoselective conjugation by azide-alkyne coupling, while allowing upturn of chitosan{\textquoteright}s amines after dephthaloylation. N-phthaloylchitosan was prepared according to previously described methods and, due to its low solubility in current organic media, subsequent modifications were run in heterogeneous conditions. Activation of hydroxyls with carbonyl-1,1'- diimidazole and coupling to propargylamine yielded N-phthaloyl-chitosan O-prop-2-ynyl carbamate, then coupled to a model PEG-like azide by azide-alkyne coupling, giving the expected triazolyl conjugate. N-Dephthaloylation allowed recovery of the free amines, responsible for chitosan{\textquoteright}s bioadhesion and tissue-regeneration properties. The structures of all polymers were confirmed by Fourier-transformed infra-red (FT-IR) and X-ray photoelectron (XPS) spectroscopies, as well as by solid-state nuclear magnetic resonance (SSNMR). All chitosan derivatives were poorly soluble in both aqueous and organic media, which makes them suitable for topical applications or for removal of toxic substances from either the gastric intestinal tract or environmental sources. {\textcopyright} 2011 Elsevier Ltd. All Rights Reserved.},
	keywords = {1 ,3-Dipolarcycloaddition, Acetylene, Amines, Azide-alkyne coupling, Bio-adhesion, Bioadhesion, Biomaterials, chitosan, click chemistry, Cycloaddition, FTIR, Huisgen{\textquoteright}s 1,3-dipolar cycloaddition, Nuclear magnetic resonance, Nuclear magnetic resonance spectroscopy, Photoelectron spectroscopy, Resonance, Size exclusion chromatography, Size-exclusion chromatography, Solid state NMR, Solid-state NMR, Tissue, X ray photoelectron spectroscopy, XPS},
	isbn = {01448617 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-80054771159\&partnerID=40\&md5=3760f41563573759f0ce676fe813d6c6},
	author = {Oliveira, J.R. and Martins, M.C.L. and Mafra, L. and Gomes, P.}
}
@article {2236,
	title = {Covalent immobilization of antimicrobial peptides (AMPs) onto biomaterial surfaces},
	journal = {Acta BiomaterialiaActa Biomater.},
	volume = {7},
	year = {2011},
	note = {Cited By (since 1996): 24Export Date: 21 November 2012Source: Scopusdoi: 10.1016/j.actbio.2010.11.005PubMed ID: 21056701Language 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: amoxicillin, 26787-78-0, 34642-77-8, 61336-70-7; ampicillin, 69-52-3, 69-53-4, 7177-48-2, 74083-13-9, 94586-58-0; carbenicillin, 17230-86-3, 4697-36-3, 4800-94-6; cefazolin, 25953-19-9, 27164-46-1; gentamicin, 1392-48-9, 1403-66-3, 1405-41-0; penicillin G, 1406-05-9, 61-33-6; teicoplanin, 61036-62-2, 61036-64-4; tobramycin, 32986-56-4; vancomycin, 1404-90-6, 1404-93-9; Antimicrobial Cationic Peptides; Biocompatible Materials; Coated Materials, Biocompatible; Immobilized ProteinsReferences: Glinel, K., Jonas, A.M., Jouenne, T., Leprince, J., Galas, L., Huck, W.T., Antibacterial and antifouling polymer brushes incorporating antimicrobial peptide (2009) Bioconj Chem, 20 (1), pp. 71-77;Vila, J., Soriano, A., Mensa, J., Molecular basis of microbial adherence to prosthetic materials. Role of biofilms in prosthesis-associated infection (2008) Enferm Infecc Microbiol Clin, 26 (1), pp. 48-54; 
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},
	month = {2011///},
	pages = {1431 - 1440},
	abstract = {Bacterial adhesion to biomaterials remains a major problem in the medical devices field. Antimicrobial peptides (AMPs) are well-known components of the innate immune system that can be applied to overcome biofilm-associated infections. Their relevance has been increasing as a practical alternative to conventional antibiotics, which are declining in effectiveness. The recent interest focused on these peptides can be explained by a group of special features, including a wide spectrum of activity, high efficacy at very low concentrations, target specificity, anti-endotoxin activity, synergistic action with classical antibiotics, and low propensity for developing resistance. Therefore, the development of an antimicrobial coating with such properties would be worthwhile. The immobilization of AMPs onto a biomaterial surface has further advantages as it also helps to circumvent AMPs{\textquoteright} potential limitations, such as short half-life and cytotoxicity associated with higher concentrations of soluble peptides. The studies discussed in the current review report on the impact of covalent immobilization of AMPs onto surfaces through different chemical coupling strategies, length of spacers, and peptide orientation and concentration. The overall results suggest that immobilized AMPs may be effective in the prevention of biofilm formation by reduction of microorganism survival post-contact with the coated biomaterial. Minimal cytotoxicity and long-term stability profiles were obtained by optimizing immobilization parameters, indicating a promising potential for the use of immobilized AMPs in clinical applications. On the other hand, the effects of tethering on mechanisms of action of AMPs have not yet been fully elucidated. Therefore, further studies are recommended to explore the real potential of immobilized AMPs in health applications as antimicrobial coatings of medical devices. {\textcopyright} 2010 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.},
	keywords = {Amino Acid Sequence, amoxicillin, ampicillin, Animals, antibiotic agent, antibiotic resistance, Antimicrobial Cationic Peptides, Antimicrobial peptides, Bacteria (microorganisms), Bacterial adhesion, bacterial survival, Biocompatible Materials, biofilm, Biofilms, biomaterial, carbenicillin, cefazolin, Coated Materials, Biocompatible, Cytotoxicity, drug activity, drug half life, drug solubility, drug stability, drug targeting, gentamicin, human, Humans, Immobilized Proteins, Molecular Sequence Data, mouth inflammation, Nanostructured surfaces, nonhuman, penicillin G, polypeptide antibiotic agent, priority journal, review, sepsis, skin infection, soft tissue infection, Surface functionalization, Surface Properties, teicoplanin, tobramycin, vancomycin},
	isbn = {17427061 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-79952187401\&partnerID=40\&md5=70d486a4c6e1ba88f804c0f0d4f4e510},
	author = {Costa, F. and Carvalho, I.F. and Montelaro, R.C. and Gomes, P. and Martins, M.C.L.}
}
