Characterization of a Crosslinked Elastomeric‐Protein Inspired Polypeptide. Issue 8 (12th July 2016)

• Record Type: Journal Article
• Authors: Bochicchio, Brigida; Bracalello, Angelo; Pepe, Antonietta
• Is Part Of: Chirality. Volume 28:Issue 8(2016)
• Page Start: 606
• Page End: 611
• Publication Date: 2016-07-12
• Subjects: AFM -- circular dichroism -- resilin -- elastin -- SEM; Chirality -- Periodicals; Pharmaceutical chemistry -- Periodicals; 541.22
• DOI: 10.1002/chir.22619
• Languages: English
• ISSNs: 0899-0042

Abstract

Abstract: Materials inspired by natural proteins have a great appeal intissue 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. Abstract : CD spectra of REC polypeptide after cross‐linking show an ensemble of conformations in aqueous solution (blue colour) and a stable type I beta‐turn in TFE (red colour). At supramolecular level, the highly regular porous structure of the cross‐linked polypeptide provides the formed hydrogel with suitable properties as scaffold in tissue engineering