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Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
Published on: August 20, 2018
Chirality Interplay of Peptide and Saccharide on Glycopeptide Self-Assembly
Limin Chen1, Xiao Zhou1,2, Yingying Huang3
1Zhejiang Engineering Research Center for Tissue Repair Materials and Wenzhou Key Laboratory of Biomaterials and Engineering and Wenzhou Key Laboratory of Biophysics, Wenzhou Institute, University of Chinese Academy of Sciences, Wenzhou 325001, China.
None:
Saccharides and peptides with markedly disparate stereochemical features serve as pivotal chiral molecular partners in living systems. The importance of glycosylation in influencing glycopeptide self-assembly has been recognized. However, how different chiral combinations of saccharides and peptides influence the macroscopic hydrogel mechanics, fiber nanomechanics, asymmetric molecular packing, and thermodynamic changes during glycopeptide self-assembly remains unknown. This study demonstrates that, following d-glycosylation of peptides, the resulting glycopeptides (L/D vs D/D) exhibited unexpected chiral self-assembly into obviously asymmetric helical nanostructures. A systematic comparative study revealed significant differences in hydrogel viscoelasticity, Young's modulus, supramolecular chiral morphologies, internal molecular stacking modes, and aggregation thermodynamics. Theoretical results indicated a strong correlation between distinct helical morphologies and interior glycopeptide stacking patterns. These findings illustrate that the chiral interplay of saccharide and peptide determines the glycopeptide supramolecular helicity. Unraveling the interplay between peptide and saccharide chirality is valuable for the precise control of the chiral self-assembly of glycopeptides.
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