Inhibition of aggregation of a biomimic peptidolipid Langmuir monolayer by Congo red studied by UV-vis and infrared spectroscopies |
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Authors: | Hasegawa Takeshi Sato Yoshiko Okada Tetsuo Shibukawa Masami Li Changqing Orbulescu Jhony Leblanc Roger M |
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Affiliation: | Department of Chemistry, Graduate School of Science and Engineering, Tokyo Institute of Technology, 2-12-1 Ookayama, Meguro-ku, Tokyo 152-8551, Japan. hasegawa@ chem.titech.ac.jp |
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Abstract: | 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. |
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