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The regulation of natural helical nanostructures is principally supported and actuated by hydrogen bonds (H-bonds) formed from hydrogen-bonding groups (peptide bonds and base pairs) to realize biological activities and specific biofunctional transformations. However, studying the role of H-bonding patterns on the handedness of supramolecular assemblies is still challenging, since supramolecular assemblies will be disassembled or destabilized with slightly varying H-bonding groups for most supramolecules. To circumvent this issue, herein, two types of self-assembled C2-symmetric phenylalanine derivatives differed by a single H-bonding group (ester or amide) are systematically designed for deciphering the role of H-bonding pattern on the chirality of supramolecular assemblies and their related biostability. Opposite handedness nanofibrous structures with tailorable diameter and helical pitch are achieved with the transition from ester to amide groups in the gelators. Experimental and theoretical evidence suggests that helical orientation of ester-containing gelators ascribes to intermolecular H-bonds. In contrast, the helical direction for the amide-counterparts is mainly due to intra- and intermolecular H-bonds. Moreover, these H-bonding groups greatly influence their stability, as revealed by in vitro and in vivo degradation experiments and the left-handed assemblies are more stable than the right-handed ones. Thus, the study offers a feasible model to have valuable insight into understanding the role of H-bonding patterns in biological folding.

Publication history
Copyright
Acknowledgements

Publication history

Received: 22 May 2021
Revised: 07 July 2021
Accepted: 16 July 2021
Published: 28 August 2021
Issue date: March 2022

Copyright

© Tsinghua University Press and Springer-Verlag GmbH Germany, part of Springer Nature 2021

Acknowledgements

Acknowledgements

This work was supported by the Innovation Program of Shanghai Municipal Education Commission (No. 201701070002E00061), the National Natural Science Foundation of China (Nos. 51833006, 52003072, 51573092, 11774078 and U1804251), and the National Key Research and Development Program of China (Nos. 2017YFB0702500 and 2016YFC1102400), and also supported by National Supercomputing Center in Zhengzhou.

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