71809-11-5Relevant academic research and scientific papers
Aggregation Behaviour of Synthetic Peptide Surfactants
Murakami, Yukito,Nakano, Akio,Iwamoto, Kiyoshi,Yoshimatsu, Akira
, p. 1809 - 1814 (2007/10/02)
Single-chain surfactants with an amino-acid residue as part of a hydrophobic chain, SS'-bis-α-(6-trimethylammoniohexanoyl)-L-hemicysteinamide> bromide +C5CysC12)2>, N-dodecyl-Nα-(6-trimethylammoniohexanoyl)-S-benzyl-L-cysteinamide bromide +C5Cys(Bzl)C12>, and N-dodecyl-Nα-(6-trimethylammoniohexanoyl)-L-aspartamide bromide (N+C5AspC12) have been synthesized and the structures of the aggregates formed in aqueous media investigated.The peptide surfactants form tighter aggregates than ordinary micelles formed with octadecyltrimethylammonium chloride.The weight-average molecular weights of the aggregates in aqueous media were determined by the low angle laser light scattering technique: N+C5Cys(Bzl)C12, 7.04*1E6; (N+C5CysC12)2, 1.49*1E6; N+C5AspC12, 5.06*1E4.Consequently, N+C5AspC12 forms tight spherical micelles while (N+C5CysC12)2 and N+C5(Bzl)C12 constitute tight and large cylindrical micelles.This aggregation behaviour was also confirmed by elctronmicroscopy.The introduction of an amino-acid residue into the hydrophobic chain of a surfactant result in tightening of the aggregate structure in aqueous media, probably due to intermolecular hydrogen bonding among amino-acid moieties in the micelle.
