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Updated: Jan 31, 2026

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility
Published on: September 6, 2024
Silver Ion-Histidine Interplay Switches Peptide Hydrogel from Antiparallel to Parallel β-Assembly and Enables
Yuchen Guo1,2, Sha Wang1,3, Hanhan Du1,3
1CAS Key Laboratory of Nano-Bio Interface, Division of Nanobiomedicine , Suzhou Institute of Nano-Tech and Nano-Bionics, Chinese Academy of Sciences , 398 Ruoshui Road, Suzhou Industrial Park , Suzhou , Jiangsu 215123 , People's Republic of China.
Abstract:
Understanding the chemical absorption process of silver ions helps the rational design of functional materials for effective release to minimize unwanted toxicity. To this end, a histidine-containing aliphatic peptide (IH6) was designed to immobilize the silver ion (Ag+) through coordinate interaction. Using circular dichroism spectroscopy, Ag+ was found to dose-dependently induce parallel β-sheet conformation of IH6 to a saturation molar ratio of 1:2. A conformational switch of IH6 from antiparallel to parallel β-sheet assembly upon Ag + coordination was further revealed by Fourier transform infrared spectroscopy. The resultant Ag-IH6 hydrogel displayed substantially enhanced mechanical strength as well as controlled release of Ag+. Ag-IH6 hydrogel thus exhibited strong dose-dependent bactericidal activities that can be tuned selectively, sparing the cocultured human keratinocytes in normal. Overall, the study demonstrates an unusual silver ion-induced peptide conformational switch between β-structure subtypes and the bilateral effects on hydrogel-based chemical control of silver ion absorption and release, thus, revealing the potential in antibacterial applications.
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