Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/12789

TitleAntimicrobial functionalized genetically engineered spider silk
Author(s)Gomes, Sílvia C.
Leonor, I. B.
Mano, J. F.
Reis, R. L.
Kaplan, David
KeywordsSpider silk
Antimicrobial activity
Recombinant proteins
Self-assembly
Cell viability
Bone tissue engineering
Issue dateJun-2011
PublisherElsevier
JournalBiomaterials
Abstract(s)Genetically engineered fusion proteins offer potential as multifunctional biomaterials for medical use. Fusion or chimeric proteins can be formed using recombinant DNA technology by combining nucleotide sequences encoding different peptides or proteins that are otherwise not found together in nature. In the present study, three new fusion proteins were designed, cloned and expressed and assessed for function, by combining the consensus sequence of dragline spider silk with three different antimicrobial peptides. The human antimicrobial peptides human neutrophil defensin 2 (HNP-2), human neutrophil defensins 4 (HNP-4) and hepcidin were fused to spider silk through bioengineering. The spider silk domain maintained its self-assembly features, a key aspect of these new polymeric protein biomaterials, allowing the formation of b-sheets to lock in structures via physical interactions without the need for chemical crosslinking. These new functional silk proteins were assessed for antimicrobial activity against Gram e Escherichia coli and Gram þ Staphylococcus aureus and microbicidal activity was demonstrated. Dynamic light scattering was used to assess protein aggregation to clarify the antimicrobial patterns observed. Attenuated-total reflectance Fourier transform infrared spectroscopy (ATR-FTIR) and circular dichroism (CD) were used to assess the secondary structure of the new recombinant proteins. In vitro cell studies with a human osteosarcoma cell line (SaOs-2) demonstrated the compatibility of these new proteins with mammalian cells.
TypeArticle
URIhttp://hdl.handle.net/1822/12789
DOI10.1016/j.biomaterials.2011.02.040
ISSN0142-9612
Publisher versionhttp://www.sciencedirect.com/
Peer-Reviewedyes
AccessOpen access
Appears in Collections:3B’s - Artigos em revistas/Papers in scientific journals

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