ABSTRACT Based on peptide sequences Ala-Aib-Ala from antibiotic Alamethicin-50 residue 9-11 and Ala-Aib-Gly from antibiotic Suzukacillin A residue 6-8, we synthesized two peptides and explored the formation of gel in various solvents. The terminally protected tripeptide Ala-Aib-Ala 1 forms a transparent gel in aromatic solvents, whereas the analogue tripeptide Ala-Aib-Gly 2 fails to form gel. FE-SEM images of the gel exhibit flake-like morphology. Rheology studies show that the storage modulus was approximately one order of magnitude larger than the loss modulus, indicating the gel`s physical crosslink. The gel is thixotropic in nature. The tripeptide 1 adopts β-turn conformation and self-assemble through intermolecular hydrogen bonds to form a supramolecular sheet-like structure in solid state. The peptide 1 gel exhibits syneresis under appropriate conditions. Moreover, the gel surfaces show an anti-sticking effect against ice and water.
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