Autori: Takeshi Hasegawa, Yoshiko Sato, Tetsuo Okada, Masami Shibukawa, Changqing Li, Jhony Orbulescu, and Roger M. Leblanc

Editorial: ACS Press, Journal of Physical Chemistry B, 111 (51), p.14227 -142, 2007.

Rezumat:

A synthetic peptidolipid consisted of a hydrocarbon chain with a chain length of C18 and a peptide moiety of IIGLM terminated with an amine group, designated as C18IIGLM-NH2, has been employed as a biomimic model compound of amyloid peptide for exploring molecular interaction and orientation with the use of the Langmuir monolayer and Langmuir-Blodgett film techniques. Inspired by a well-known fact that a stain reagent, Congo red (CR), binds well to the amyloid-mimic part (IIGLM), inhibition of molecular aggregation of C18IIGLM-NH2 by interaction with CR was expected, and it has been investigated by use of surface pressure-area isotherm, surface dipole moment-area isotherm, Brewster-angle microscopy, and UV-vis/infrared spectroscopies. It has been revealed that monomeric CR molecules whose long axis is parallel to the Langmuir monolayer surface are penetrating the C18IIGLM-NH2 Langmuir monolayer, which plays a role of inhibition of molecular aggregation via hydrogen bonding.

Cuvinte cheie: amyloid aggregation and inhibition, Congo red, UV-Vis, FTIR, MAIRS, Langmuir film, surface chemistry

URL: http://pubs.acs.org/cgi-bin/abstract.cgi/jpcbfk/2007/111/i51/abs/jp0759269.html