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Characterization of a Crosslinked Elastomeric-Protein Inspired Polypeptide.
Bochicchio, Brigida; Bracalello, Angelo; Pepe, Antonietta.
Afiliação
  • Bochicchio B; Laboratory of Protein-Inspired Materials, Department of Science, University of Basilicata, Potenza, Italy.
  • Bracalello A; Laboratory of Protein-Inspired Materials, Department of Science, University of Basilicata, Potenza, Italy.
  • Pepe A; Laboratory of Protein-Inspired Materials, Department of Science, University of Basilicata, Potenza, Italy.
Chirality ; 28(8): 606-11, 2016 08.
Article em En | MEDLINE | ID: mdl-27403636
Materials inspired by natural proteins have a great appeal in tissue engineering for their biocompatibility and similarity to extracellular matrix (ECM). Chimeric polypeptides inspired by elastomeric proteins such as silk, elastin, and collagen are of outstanding interest in the field. A recombinant polypeptide constituted of three different blocks, each of them having sequences derived from elastin, resilin, and collagen proteins, was demonstrated to be a good candidate as biomaterial for its self-assembling characteristics and biocompatibility. Herein, taking advantage of the primary amine functionalities present in the linear polypeptide, we crosslinked it with 1,6-hexamethylene-diisocyanate (HMDI). The characterization of the obtained polypeptide was realized by CD spectroscopy, AFM, and SEM microscopies. The obtained results, although not conclusive, demonstrate that the crosslinked polypeptide gave rise to porous networks, thin nanowires, and films not observable for the linear polypeptide. Chirality 28:606-611, 2016. © 2016 Wiley Periodicals, Inc.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos / Proteínas Recombinantes / Isocianatos / Reagentes de Ligações Cruzadas Idioma: En Ano de publicação: 2016 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos / Proteínas Recombinantes / Isocianatos / Reagentes de Ligações Cruzadas Idioma: En Ano de publicação: 2016 Tipo de documento: Article