Metal-Promoted Assembly of Two Collagen Mimetic Peptides into a Biofunctional -Spiraled Horn- ScaffoldReport as inadecuate


Metal-Promoted Assembly of Two Collagen Mimetic Peptides into a Biofunctional -Spiraled Horn- Scaffold


Metal-Promoted Assembly of Two Collagen Mimetic Peptides into a Biofunctional -Spiraled Horn- Scaffold - Download this document for free, or read online. Document in PDF available to download.

Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN 47907, USA





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Academic Editor: Fabio Nudelman

Abstract Biofunctional scaffolds for the delivery of living cells are of the utmost importance for regenerative medicine. Herein, a novel, robust -spiraled horn- scaffold was elucidated through the Co2+-promoted hierarchical assembly of two collagen mimetic peptides, NCoH and HisCol. Each -horn- displayed a periodic banding pattern with band lengths corresponding to the length of the collagen peptide triple helix. Strand exchange between the two peptide trimers resulted in failure to form this intricate morphology, lending support to a precise metal-ligand-based mechanism of assembly. Little change occurred to the observed morphology when the Co2+ concentration was varied from 0.5 to 4.0 mM, and the scaffold was found to be fully formed within two minutes of exposure to the metal ion. The horned network also displayed biological functionality by binding to a His-tagged fluorophore and associating with cells. View Full-Text

Keywords: collagen mimetic peptides; hierarchical assembly; biomimetic scaffold collagen mimetic peptides; hierarchical assembly; biomimetic scaffold





Author: Kevin Strauss and Jean Chmielewski *

Source: http://mdpi.com/



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