Hydrogelation of cyclic peptide amphiphile, colistin, through formation of hierarchically organized structure
July 31-August 4, 2017
Colistin (Col) is an cationic amphiphilic molecule having a cyclic peptide moiety as a hydrophilic group. Because of such a unique molecular architecture, self-assembled structure of Col should be much different from that of a linear amphiphilic peptide. Especially, effect of pH on self-assembly in aqueous Col solution is interesting because inter- and intra-ring interactions of Col should be affected with pH change. Thus, in this study, we investigated self-assembly of Col in aqueous solution with various pH by using small-angle X-ray scattering (SAXS) with synchrotron light source.
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Kosuke Morimoto, Satoshi Kanazawa, and Isamu Akiba, "Hydrogelation of cyclic peptide amphiphile, colistin, through formation of hierarchically organized structure" in "Association in Solution IV", Ulf Olsson, Lund University, Sweden Norman Wagner, University of Delaware, USA Anand Yethiraj, Memorial University of Newfoundland, Canada Eds, ECI Symposium Series, (2017). http://dc.engconfintl.org/assoc_solution_iv/10
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