General Solution for Stabilizing Triple Helical Collagen

被引:39
作者
Zhang, Yitao [1 ]
Herling, Madison [1 ]
Chenoweth, David M. [1 ]
机构
[1] Univ Penn, Dept Chem, 231 South 34th St, Philadelphia, PA 19104 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
CONFORMATIONAL STABILITY; OSTEOGENESIS IMPERFECTA; MODEL PEPTIDES; GLYCINE; RESIDUES; DISEASES; RING;
D O I
10.1021/jacs.6b03823
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
One of the most ubiquitous stabilizing forces in nature is the hydrogen bond, exemplified by the folded secondary, tertiary, and higher-order structure of biomolecules. Despite the fundamental importance of hydrogen bonding, dependence on this stabilizing force places limitations on nature's proteinogenic building blocks. Herein, we demonstrate that replacement of the strictly conserved glycine in collagen with aza-glycine has profound consequences on the stability and self-assembly of collagen peptides by providing an extra hydrogen bond donor. The additional hydrogen bond provided by azaglycine allows for complete replacement of glycine residues in collagen peptides and truncation to the smallest self assembling collagen peptide systems observed to date. Our results highlight the vital importance of hydrogen bonding at desolvated interfaces, providing a new strategy for optimization of designed peptide materials and a general solution for stabilizing the collagen triple helix.
引用
收藏
页码:9751 / 9754
页数:4
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