title: Energy transfer at heterogeneous protein-protein interfaces to investigate the molecular behaviour in the crowding environment.
abstract: Investigation of the behaviour of proteins in crowded environments is crucial for understanding the role of proteins in biological environments. In this study, the behaviour of bovine serum albumin (BSA) in crowded (highly concentrated) environments was investigated using time-resolved fluorescence spectroscopy as a model system. By using energy transfer as a molecular ruler, the crowding effect was clearly observed in the time resolved spectra. In addition, by using both time resolved anisotropy measurement and Raman spectroscopy, more detail insights from conformational and dynamic points of view were described. Consequently, it was revealed that in the highly concentrated solution, most of the BSA molecules are in the fast-reversible oligomeric state and the association at the "hard" and "soft" interfaces between protein surfaces occurred in a highly crowded environment with the aid of a charge-charge and short-range attractive interface. From both the conformational and dynamic aspects, the detail spectroscopic understanding of the behaviour of BSA in the crowding environment was obtained.
authors.affiliation: Advanced R&D Center, HORIBA, Ltd., 2 Miyanohigashi, Kisshoin, Minami-ku, Kyoto 601-8510, Japan. Electronic address: chikashi.ota@horiba.com.
authors.forename: Chikashi
authors.initials: C
authors.lastname: Ota
mesh_terms: D000818:Animals; D016880:Anisotropy; D002417:Cattle; D004735:Energy Transfer; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D012996:Solutions; D013050:Spectrometry, Fluorescence; D013059:Spectrum Analysis, Raman; D013997:Time Factors
chemical_list: D012996:Solutions; D012710:Serum Albumin, Bovine
keywords: Energy transfer; Protein-protein interfaces; Time resolved fluorescence spectroscopy