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Controlling the morphology of metal‐triggered collagen peptide assemblies through ligand alteration
Author(s) -
Kotha Raghavendhar R.,
Chmielewski Jean
Publication year - 2015
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22690
Subject(s) - peptide , chemistry , ligand (biochemistry) , moiety , metal , carboxylate , morphology (biology) , stereochemistry , biophysics , crystallography , biochemistry , receptor , organic chemistry , biology , genetics
A number of methods have been explored to promote the higher order assembly of collagen peptide triple helices. In one case, NCoH , a complex hierarchical metal‐promoted assembly was observed to form micron‐scaled florettes with a ruffled surface topology at the nanoscale. In an effort to elucidate the role of the ligands in this collagen peptide assemblage, we reduced the number of carboxylates within the N‐terminal ligand to produce a new peptide, ICoH . A striking difference in the morphology of the metal‐triggered material was observed with ICoH , with stacked arrays of nanofibrils predominating. As the peptide to metal ion ratio was increased, the length of the stacks of fibrils was also observed to increase. These data demonstrate that a significantly less complex assembly process occurs with the removal of a single carboxylate moiety from the metal binding ligand at the termini of the collagen peptide. © 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 104: 379–383, 2015.