Time-resolved Fluorescence Spectroscopic Studies on the Binding of L-[4-(1-Pyrene)butyroyl]-phenylalanine with Proteins

Abstract

Abstract: Time-resolved fluorescence spectra was applied to studying the binding of L-[4-(1-pyrene)butyroyl]-phenylalanine(PLP) with lysozyme(lys), bovine serum albumin(BSA) and human serum albumin(HSA). The fluorescence lifetimes of pyrenyl group quenched by using cobalt(Ⅲ) hexaamine(CoHA) in free state and in different complexes protein systems were also investigated. These results suggest that PLP binds with SAs via its pyrenyl group insertion in the hydrophobic cavity of protein, whereas it binds with Lys in the hydrophobic area on the surface.

Key words: Time-resolved fluorescence spectroscopy, Serum albumin, L-[4-(1-Pyrene)butyroyl]-phenylalanine(PLP), Lysozyme

CLC Number:

O657

TrendMD:

CHEN Kai, ZHAI Chun-Xi, LI Wen, WU Li-Xin, WU Yu-Qing, ZHANG Jian-Ping, AI Xi-Cheng . Time-resolved Fluorescence Spectroscopic Studies on the Binding of L-[4-(1-Pyrene)butyroyl]-phenylalanine with Proteins[J]. Chem. J. Chinese Universities, 2004, 25(10): 1905.

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Time-resolved Fluorescence Spectroscopic Studies on the Binding of L-[4-(1-Pyrene)butyroyl]-phenylalanine with Proteins

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