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Open AccessArticle

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

Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN 47907, USA
Author to whom correspondence should be addressed.
Academic Editor: Fabio Nudelman
Materials 2016, 9(10), 838;
Received: 12 August 2016 / Revised: 30 September 2016 / Accepted: 11 October 2016 / Published: 17 October 2016
(This article belongs to the Special Issue Biological and Synthetic Organic–Inorganic Composite Materials)
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
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MDPI and ACS Style

Strauss, K.; Chmielewski, J. Metal-Promoted Assembly of Two Collagen Mimetic Peptides into a Biofunctional “Spiraled Horn” Scaffold. Materials 2016, 9, 838.

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