2015
DOI: 10.1039/c4mh00223g
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Transient supramolecular reconfiguration of peptide nanostructures using ultrasound

Abstract: This version is available at https://strathprints.strath.ac.uk/51770/ Strathprints is designed to allow users to access the research output of the University of Strathclyde. Unless otherwise explicitly stated on the manuscript, Copyright © and Moral Rights for the papers on this site are retained by the individual authors and/or other copyright owners. Please check the manuscript for details of any other licences that may have been applied. You may not engage in further distribution of the material for any pro… Show more

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Cited by 58 publications
(39 citation statements)
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“…Infrared (IR) spectroscopy deals with the electromagnetic spectrum change of peptides due to molecular vibrations and conformational changes within amide A (∼3200-3300 cm −1 ), amide I (∼1600-1700 cm −1 ), amide II (∼1480-1580 cm −1 ) and amide III (∼1200-1300 cm −1 ) bands in themid-infrared region [230][231][232]. The shifts in the amide I band were analysed to monitor the structural changes as a result of the peptide self-assembly, which can be triggered via different factors such as UV irradiation [233], ultrasonication [234,235], pH, ion addition or electrostatic interactions. In particular, the peaks in the amide I bands, which are correlated with C=O stretching of the self-assembled peptide nanostructures, contribute to the analysis of parallel or antiparallel β-sheet [236,237], α-helix, β-turn or random-coil secondary structure organization of the peptide assemblies.…”
Section: Spectroscopic Analysismentioning
confidence: 99%
“…Infrared (IR) spectroscopy deals with the electromagnetic spectrum change of peptides due to molecular vibrations and conformational changes within amide A (∼3200-3300 cm −1 ), amide I (∼1600-1700 cm −1 ), amide II (∼1480-1580 cm −1 ) and amide III (∼1200-1300 cm −1 ) bands in themid-infrared region [230][231][232]. The shifts in the amide I band were analysed to monitor the structural changes as a result of the peptide self-assembly, which can be triggered via different factors such as UV irradiation [233], ultrasonication [234,235], pH, ion addition or electrostatic interactions. In particular, the peaks in the amide I bands, which are correlated with C=O stretching of the self-assembled peptide nanostructures, contribute to the analysis of parallel or antiparallel β-sheet [236,237], α-helix, β-turn or random-coil secondary structure organization of the peptide assemblies.…”
Section: Spectroscopic Analysismentioning
confidence: 99%
“…Due to the reversible nature of interactions, these gels are responsive and tuneable. Responsiveness of these gels to stimuli such as light,3033 pH changes,34 ultrasound,3537 enzymes38, 39 and changes in the redox state4043 is of particular interest. In order to design such “smart peptide materials”, it is important to have a thorough understanding of the intermolecular interactions that control the self‐assembly and consequent architecture of the material and its bulk properties.…”
Section: Introductionmentioning
confidence: 99%
“…Ultrasound has also been used as a dissipative force or thermodynamic accelerator in controlling supramolecular structures. For example, ultrasound can be used to overcome kinetic barriers and enable reversible reconfiguration of a peptide nanostructure, promote disassembly of supramolecular micellar structures, or induce reversible polymerization or gelation in a supramolecular material . The clinical use of high‐intensity focused ultrasound suggests that ultrasound‐mediated control of supramolecular materials could have broad relevance for therapeutic application, and this approach certainly warrants further consideration in designing “smart” therapies.…”
Section: Preparing Responsive Supramolecular Materialsmentioning
confidence: 99%