Chemistry and Physics Faculty Articles

Document Type

Article

Publication Date

7-26-2021

Publication Title

Small

ISSN

1613-6829

First Page

2102525

Abstract

The synthesis of morphologically well-defined peptidic materials via self-assembly is challenging but demanding for biocompatible functional materials. Moreover, switching morphology from a given shape to other predictable forms by molecular modification of the identical building block is an even more complicated subject because the self-assembly of flexible peptides is prone to diverge upon subtle structural change. To accomplish controllable morphology transformation, systematic self-assembly studies are performed using congener short β-peptide foldamers to find a minimal structural change that alters the self-assembled morphology. Introduction of oxygen-containing β-amino acid (ATFC) for subtle electronic perturbation on hydrophobic foldamer induces a previously inaccessible solid-state conformational split to generate the most susceptible modification site for morphology transformation of the foldamer assemblies. The site-dependent morphological switching power of ATFC is further demonstrated by dual substitution experiments and proven by crystallographic analyses. Stepwise morphology transformation is shown by modifying an identical foldamer scaffold. This study will guide in designing peptidic molecules from scratch to create complex and biofunctional assemblies with nonspherical shapes.

Comments

This work was supported by the National Research Foundation of Korea (NRF) grants funded by the Korea government (MSIT and Ministry of Education) (No. 2018R1A5A1025208 and No. 2019R1A61A10073887). R.W.D. acknowledges a President's Faculty Research and Development Grant (No. 334835). The synchrotron powder and single-crystal X-ray diffraction data for structure determination were collected from the 9B and 2D beamline at the Pohang Accelerator Laboratory (Pohang, Republic of Korea), respectively.

Additional Comments

© 2021 The Authors. Small published by Wiley-VCH GmbH. This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

ORCID ID

0000-0003-2470-9164

DOI

10.1002/smll.202102525

Peer Reviewed

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