Journal article
Short Peptides as Tunable, Switchable, and Strong Gelators
The journal of physical chemistry. B, v 125(25), pp 6760-6775
01 Jul 2021
PMID: 34133176
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
This Perspective outlines our current understanding of molecular gels composed of short and ultrashort peptides over the past 20 years. We discuss in detail the state of the art regarding self-assembly mechanisms, structure, thermal stability, and kinetics of fibril and/or network formation. Emphasis is put on the importance of the combined use of spectroscopy and rheology for characterizing and validating self-assembly models. While a range of peptide chemistries are reviewed, we focus our discussion on a unique new class of ultrashort peptide gelators, denoted GxG peptides (x: guest residue), which are capable of forming self-assembled fibril networks. The storage moduli of GxG gels are tunable up to 100 kPa depending on concentration, pH, and/or cosolvent. The sheet structures of the fibrils differ from canonical beta-sheets. When appropriate, each section highlights opportunities for additional research and technologies that would further our understanding.
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Details
- Title
- Short Peptides as Tunable, Switchable, and Strong Gelators
- Creators
- Reinhard Schweitzer-Stenner - Drexel UniversityNicolas J. Alvarez - Drexel University
- Publication Details
- The journal of physical chemistry. B, v 125(25), pp 6760-6775
- Publisher
- American Chemical Society; Washington, DC
- Number of pages
- 16
- Grant note
- DMR-1707770 / National Science Foundation; National Science Foundation (NSF)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]; Chemical and Biological Engineering
- Web of Science ID
- WOS:000670636400004
- Scopus ID
- 2-s2.0-85111770531
- Other Identifier
- 991019167880504721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Chemistry, Physical