Hydrogelation of cyclic peptide amphiphile, colistin, through formation of hierarchically organized structure

Conference Dates

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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