By a News Reporter-Staff News Editor at Life Science Weekly -- Fresh data on Proteomics are presented in a new report. According to news reporting originating from Regensburg, Germany, by NewsRx correspondents, research stated, "This work demonstrates that the incorporation of azobenzene residues into the side chain of low-molecular-weight peptides can modulate their self-assembly process in organic solvents leading to the formation of stimuli responsive physical organogels. The major driving forces for the gelation process are hydrogen bonding and - interactions, which can be triggered either by thermal or ultrasound external stimuli, affording materials having virtually the same properties."
Our news editors obtained a quote from the research from the University of Regensburg, "In addition, a predictive model for gelation of polar protic solvent was developed by using Kamlet-Taft solvent parameters and experimental data. The obtained viscoelastic materials exhibited interconnected multistimuli responsive behaviors including thermal-, photo-, chemo- and mechanical responses. All of them displayed thermoreversability with gel-to-sol transition temperatures established between 33-80 degrees C and gelation times from minutes to several hours. Structure-property relationship studies of a designed peptide library have demonstrated that the presence and position of the azobenzene residue can be operated as a versatile regulator to reduce the critical gelation concentration and enhance both the thermal stability and mechanical strength of the gels, as demonstrated by comparative dynamic rheology. The presence of N-Boc protecting group in the peptides showed also a remarkable effect on the formation and properties of the gels. Despite numerous examples of peptide-based gelators known in the literature, this is the first time in which low-molecular-weight peptides bearing side chain azobenzene units are used for the synthesis of intelligent supramolecular organogels."
According to the news editors, the research concluded: "Compared with other approaches, this strategy is advantageous in terms of structural flexibility since it is compatible with a free, unprotected amino terminus and allows placement of the chromophore at any position of the peptide sequence."
For more information on this research see: Multistimuli-Responsive Supramolecular Organogels Formed by Low-Molecular-Weight Peptides Bearing Side-Chain Azobenzene Moieties. Chemistry-A European Journal, 2013;19(27):8861-8874. Chemistry-A European Journal can be contacted at: Wiley-V C H Verlag Gmbh, Boschstrasse 12, D-69469 Weinheim, Germany (see also Proteomics).
The news editors report that additional information may be obtained by contacting P. Fatas, University of Regensburg, Inst Organ Chem, D-93053 Regensburg, Germany. Additional authors for this research include J. Bachl, S. Oehm, A.I. Jimenez, C. Cativiela and D.D. Diaz.
Keywords for this news article include: Europe, Germany, Peptides, Proteins, Regensburg, Proteomics, Amino Acids, Nanotechnology, Supramolecular, Emerging Technologies
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