Chem. J. Chinese Universities

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Study on Interfacial Adsorption Behavior of Bovine Serum Albumin on Air-water Interface and Its Interaction with Chiral Probes D/L-N-[4-(1-Pyrene)butyroyl]-phenylalanine

ZHAI Chun-Xi, MA Li-Jun, LI Li-Na, WU Yu-Qing, LI Wen, WU Li-Xin   

  1. Key Laboratory for Supramolecular Structure and Materials of Ministry of Education, Jilin University, Changchun 130012, China
  • Received:2005-06-28 Revised:1900-01-01 Online:2006-08-10 Published:2006-08-10
  • Contact: WU Yu-Qing

Abstract: Surface pressure vs. time(π-t) curve was applied to studing the interfacial adsorption behavior of bovine serum albumin(BSA) and the chiral discrimination of it to D/L-N-[4-(1-pyrene)butyroyl] phenylalanine(PPs) on the air/water interface. The conformational changes of BSA induced by the interactions with PPs were also investigated. The results suggest that stable monolayer of BS underwent a slow progress of conformational rearrangement. It is apparent that the specific interactions between PPs and BSA depend both on the concentration and the isomeric specificity of the probes. At a high concentration, PLP and PDP inhibit the surface activity of BSA strongly. However, at a certain low concentration, they work oppositely. And compared with PLP, PDP can bind more effectively with BSA on the air/water interface.

Key words: π-t curves, Bovine serum albumin(BSA), L-N-[4-(1-pyrene)butyroyl] phenylalanine(PLP), D-N-[4-(1-pyrene)butyroyl] phenylalanine(PDP), Surface interaction

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