View in EDS

Synergistic anion-π interactions in peptidomimetic polyethers.

Saved in:
Bibliographic Details
Title: Synergistic anion-π interactions in peptidomimetic polyethers.
Authors: Seunghyun Lee1, Aram Shin2, Jinwoo Park1, Sowon Yun2, Minseong Kim2 mskim94@yonsei.ac.kr, Dong Woog Lee1 dongwoog.lee@unist.ac.kr, Byeong-Su Kim2 bskim19@yonsei.ac.kr
Source: Proceedings of the National Academy of Sciences of the United States of America. 2/11/2025, Vol. 122 Issue 6, p1-7. 26p.
Subjects: Ring-opening polymerization, Polyethers, Addition polymerization, Phenyl group, Aspartic acid
Abstract: Anion-π interactions are crucial in various biological processes, such as enzyme catalysis and ion transport. Despite their significance, the exploitation of anion-π interactions in synthetic polymer systems remains underexplored. This study investigates anion-π interactions using chemically well-defined peptidomimetics guided by the composition of mussel foot proteins. Specifically, polyether-based polymers were designed utilizing two functional epoxide monomers--catechol acetonide glycidyl ether and 4,4-dimethyl- 2- oxazoline glycidyl ether--to mimic the key amino acids 3,4-dihydroxyphenylalanine and aspartic acid, respectively. A surface forces apparatus was employed to study the anion-π interaction between the polymers, considering the effects of relative monomer composition and pH conditions. The maximum cohesion energy of 15.0 mJ/m2 was observed at an equimolar monomer composition at pH 7. Incorporating a phenyl group instead of the catechol group and introducing competing anions confirmed the dominant role of anion-π interactions. This study highlights the significance of anion-π interactions, posing a high potential in the design and synthesis of functional materials. [ABSTRACT FROM AUTHOR]
Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
Description
Abstract:Anion-π interactions are crucial in various biological processes, such as enzyme catalysis and ion transport. Despite their significance, the exploitation of anion-π interactions in synthetic polymer systems remains underexplored. This study investigates anion-π interactions using chemically well-defined peptidomimetics guided by the composition of mussel foot proteins. Specifically, polyether-based polymers were designed utilizing two functional epoxide monomers--catechol acetonide glycidyl ether and 4,4-dimethyl- 2- oxazoline glycidyl ether--to mimic the key amino acids 3,4-dihydroxyphenylalanine and aspartic acid, respectively. A surface forces apparatus was employed to study the anion-π interaction between the polymers, considering the effects of relative monomer composition and pH conditions. The maximum cohesion energy of 15.0 mJ/m2 was observed at an equimolar monomer composition at pH 7. Incorporating a phenyl group instead of the catechol group and introducing competing anions confirmed the dominant role of anion-π interactions. This study highlights the significance of anion-π interactions, posing a high potential in the design and synthesis of functional materials. [ABSTRACT FROM AUTHOR]
ISSN:00278424
DOI:10.1073/pnas.2419404122