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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
Published on: February 6, 2020
Chirality Inversion upon Coassembly of Stereoisomeric Short Peptides with Like-Handedness.
Yan Wang1, Yurong Zhao1, Henghao Yu1
1Department of Biological and Energy Chemical Engineering, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao 266580, China.
Chirality inversion during coassembly of two different peptide stereoisomers was observed. This phenomenon, driven by structural flexibility and component ratios, enables control over supramolecular chirality in peptide bionanomaterials.
Area of Science:
- Supramolecular chemistry
- Bionanomaterials science
- Peptide self-assembly
Background:
- Chirality inversion is well-documented for single chiral component self-assembly.
- Coassembly of multiple chiral components and subsequent chirality inversion remains underexplored.
Purpose of the Study:
- To investigate supramolecular chirality inversion in the coassembly of two distinct stereoisomers of an amphiphilic peptide.
- To understand the mechanisms governing chirality inversion during coassembly.
Main Methods:
- Coassembly of two different stereoisomers of an amphiphilic I3K peptide sequence.
- Characterization of self-assembled nanofibrils.
- Theoretical simulations to elucidate structural and bonding mechanisms.
Main Results:
- Coassembled nanofibrils exhibited significant helix inversion compared to individual peptide nanofibrils across various mixing ratios.
- Theoretical simulations indicated that structural flexibility facilitates interstrand H-bonding, leading to chirality inversion in mixed β-sheets.
- Inverted strands with heterogeneous interfaces showed increased twisting, inducing helix inversion in the overall structure.
Conclusions:
- Supramolecular chirality inversion can be achieved through the coassembly of different peptide stereoisomers.
- The ratio of components is a key factor in regulating the helix inversion of the final nanofibrils.
- This work provides a foundation for controlling suprastructure chirality in peptide bionanomaterials via coassembly.
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