Using a collagen heterotrimer to screen for cation-π interactions to stabilize triple helices

[Display omitted] •A mutant library of cation-π interactions to collagen stability was constructed based on a collagen heterotrimer.•Five axial and one lateral cation-π pairs showed stabilizing effects on collagen.•Axial RF pair not only had high stabilizing effects but also occurred frequently in n...

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Bibliographic Details
Published in:Chemical physics letters 2019-01, Vol.715, p.77-83
Main Authors: Zheng, Hongning, Liu, Han, Hu, Jinyuan, Xu, Fei
Format: Article
Language:English
Subjects:
Collagen
Energetic contribution
Prediction of stability
Salt bridge
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Summary:[Display omitted] •A mutant library of cation-π interactions to collagen stability was constructed based on a collagen heterotrimer.•Five axial and one lateral cation-π pairs showed stabilizing effects on collagen.•Axial RF pair not only had high stabilizing effects but also occurred frequently in natural collagen sequences. As one of non-covalent forces to stabilize protein, cation-π interactions in collagen have been received much attention. Three chains of collagen form its characteristic secondary structure, triple helices. Based on a collagen heterotrimer, abc, a library containing 15 mutant peptides was built to characterize the stabilizing effects of 24 pairwise cation-π interactions. The six stabilizing pairs, axial FK, YK, WK, RF, and RW, and lateral RF, have been identified, among which only axial RF frequently occurs in natural collagen sequences. This suggests that cation-π interactions might not be optimized in natural collagen.
ISSN:0009-2614
1873-4448
DOI:10.1016/j.cplett.2018.10.073