General Solution for Stabilizing Triple Helical Collagen.
General Solution for Stabilizing Triple Helical Collagen.
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DOI：
10.1021/jacs.6b03823
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发表时间：
2016-07
影响因子：
15
通讯作者：
Yitao Zhang;Madison R Herling;D. Chenoweth
中科院分区：
文献类型：
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作者：
Yitao Zhang;Madison R Herling;D. Chenoweth
自然界中最普遍的稳定力之一是氢键，生物分子的折叠二级、三级和高阶结构就是例证。尽管氢键很重要，但对这种稳定力量的依赖对自然界中产生蛋白质的构件构成了限制。在这里，我们证明了用氮杂甘氨酸取代胶原中严格保守的甘氨酸，通过提供额外的氢键供体，对胶原肽的稳定性和自组装产生了深远的影响。氮杂-甘氨酸提供的额外氢键可以完全取代胶原肽中的甘氨酸残基，并截断为迄今为止观察到的最小的自组装胶原肽系统。我们的结果强调了脱溶界面上氢键的重要性，为优化设计的多肽材料提供了一种新的策略，并为稳定胶原蛋白三螺旋提供了一般解决方案。
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 aza-glycine 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.