Development of a collagen-like peptide polymer via end-to-end disulfide cross-linking and its application as a biomaterial. (August 2019)

• Record Type: Journal Article
• Authors: Ichise, Shinichiro F.; Takeuchi, Shungo; Aoki, Shigehisa; Kuroda, Kazuki C.; Nose, Hiroshi; Masuda, Ryo; Koide, Takaki
• Is Part Of: Acta biomaterialia. Volume 94(2019)
• Page Start: 361
• Page End: 371
• Publication Date: 2019-08
• Subjects: ATR attenuated total reflection -- CD circular dichroism -- DIC N, N′-diisopropylcarbodiimide -- D-MEM Dulbecco's modified Eagle's medium -- DMF N, N-dimethylformamide -- DMSO dimethyl sulfoxide -- DTT 1, 4-dithiothreitol -- ECM extracellular matrix -- EDTA ethylenediaminetetraacetic acid -- FAK focal adhesion kinase -- FBS fetal bovine serum -- Fmoc 9-fluorenylmethoxycarbonyl -- FT-IR Fourier transform infrared -- GFP green fluorescence protein -- GPVI glycoprotein VI -- HOBt 1-hydroxybenzotriazole -- HRP horseradish peroxidase -- Hyp or O 4-hydroxyproline -- MALDI-TOF MS matrix-assisted laser desorption-ionization time-of-flight mass spectrometry -- MMPs matrix metalloproteinases -- PBS phosphate buffered saline -- PP-II polyproline-II -- PVDF polyvinylidene difluoride -- RP-HPLC reverse phase high performance liquid chromatography -- SPARC secreted protein acidic and rich in cysteine -- TFA trifluoroacetic acid -- Tm melting temperature of triple helix standard three or one letter codes for amino acids were used; Extracellular matrix (ECM) -- Collagen -- Triple helix -- Peptide -- Integrin; Biomedical materials -- Periodicals; 610.28
• DOI: 10.1016/j.actbio.2019.06.010
• Languages: English
• ISSNs: 1742-7061

Abstract

Graphical abstract: Abstract: Collagen is the most abundant protein in the animal kingdom and has a unique triple-helical structure. It not only provides mechanical strength to tissues, but also performs specific biological functions as a multifaceted signaling molecule. Animal-derived collagen is therefore widely used as a biocompatible material in vitro and in vivo . In this study, we developed a novel peptide-based material that mimicked both the polymeric properties and a selected biological function of native collagen. This material was prepared by end-to-end multiple disulfide cross-linking of chemically synthesized triple-helical peptides. The peptide polymer showed a gel-forming property, and receptor-specific cell binding was observed in vitro by incorporating a peptide harboring an integrin α2β1-binding sequence. Furthermore, cell signaling activity and biodegradability were tunable according to the polymer contents. The results demonstrated the potential of this material as a designer collagen. Statement of Significance: Collagen is a useful biomaterial with the gel-forming property. It also exhibits various biological activities through the interaction of specific amino acid sequences displayed on the triple helix with functional biomacromolecules. Here we report a novel synthetic material, artificial collagen, by end-to-end cross-linking of chemically synthesized collagen-like triple-helical peptides. The material allows independent regulation of polymer properties, i.e. gel stiffness, and sequence-specific bioactivities by altering peptide compositions. This material can also be variously shaped, for example, thin films with high transparency. In addition, it has low inflamatogenic properties and tunable biodegradability in vivo .