ja7b03398_si_001.pdf (10.2 MB)
Structural Basis for Aza-Glycine Stabilization of Collagen
Version 2 2017-07-14, 20:43
Version 1 2017-07-06, 16:51
journal contribution
posted on 2017-06-26, 00:00 authored by Alexander
J. Kasznel, Yitao Zhang, Yang Hai, David M. ChenowethPreviously,
we have demonstrated that replacement of the strictly
conserved glycine in collagen with aza-glycine provides a general
solution for stabilizing triple helical collagen peptides (Chenoweth,
D. M.; et al. J. Am. Chem. Soc. 2016, 138, 9751; 2015, 137, 12422). The additional hydrogen
bond and conformational constraints provided by aza-glycine increases
the thermal stability and rate of folding in collagen peptides composed
of Pro-Hyp-Gly triplet repeats, allowing for truncation to the smallest
self-assembling peptide systems observed to date. Here we show that
aza-glycine substitution enhances the stability of an arginine-containing
collagen peptide and provide a structural basis for this stabilization
with an atomic resolution crystal structure. These results demonstrate
that a single nitrogen atom substitution for a glycine alpha-carbon
increases the peptide’s triple helix melting temperature by
8.6 °C. Furthermore, we provide the first structural basis for
stabilization of triple helical collagen peptides containing aza-glycine
and we demonstrate that minimal alteration to the peptide backbone
conformation occurs with aza-glycine incorporation.
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Keywords
self-assembling peptide systemspeptide backbone conformationcollagen peptidesaza-glycine incorporationhelical collagen peptidesnitrogen atom substitutionAza-Glycine StabilizationStructural Basisarginine-containing collagen peptidePro-Hyp-Gly tripletresolution crystal structureaza-glycine substitutionglycine alpha-carbon increasesaza-glycine increaseshydrogen bond
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