Structural
Basis for Aza-Glycine Stabilization of Collagen
Alexander
J. Kasznel
Yitao Zhang
Yang Hai
David M. Chenoweth
10.1021/jacs.7b03398.s001
https://acs.figshare.com/articles/journal_contribution/Structural_Basis_for_Aza-Glycine_Stabilization_of_Collagen/5179021
Previously,
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. <i>J. Am. Chem. Soc.</i> <b>2016</b>, <i>138</i>, 9751; <b>2015</b>, <i>137</i>, 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.
2017-06-26 00:00:00
self-assembling peptide systems
peptide backbone conformation
collagen peptides
aza-glycine incorporation
helical collagen peptides
nitrogen atom substitution
Aza-Glycine Stabilization
Structural Basis
arginine-containing collagen peptide
Pro-Hyp-Gly triplet
resolution crystal structure
aza-glycine substitution
glycine alpha-carbon increases
aza-glycine increases
hydrogen bond