Deciphering the Fluorescence Resonance Energy Transfer Signature of 3-Pyrazolyl 2-Pyrazoline in Transport Proteinous Environment

被引：59

作者：

Banerjee, Paltu ^{[1
]}

Pramanik, Smiritimoy ^{[1
]}

Sarkar, Arindam ^{[1
]}

Bhattacharya, Subhash Chandra ^{[1
]}

机构：

[1] Jadavpur Univ, Dept Chem, Kolkata 700032, India

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2009年 / 113卷 / 33期

关键词：

BOVINE SERUM-ALBUMIN; BINDING; PHOTOPHYSICS; AGENTS; SITE;

D O I：

10.1021/jp811479r

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070305 [高分子化学与物理];

摘要：

In the present investigation, an attempt has been made to study the interaction of newly synthesized bioactive compound 3-pyrazolyl 2-pyrazoline (PZ) with model transport proteins, bovine serum albumin (BSA), and human serum albumin (HSA) employing steady state and time-resolved fluorescence technique. We have focused on fluorescence resonance energy transfer (FRET) between excited tryptophan in transport proteins to transport-proteins-bound PZ. An efficient Forster-type resonance energy transfer from the tryptophan residues to PZ indicates that PZ binds in the vicinity of the tryptophan residue. Binding of protein to that bioactive compound without changing conformation of primary and secondary structure of protein has been monitored using circular dichroism (CD) study.

引用

页码：11429 / 11436

页数：8

共 41 条

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Effect of albumin conformation on the binding of ciprofloxacin to human serum albumin: A novel approach directly assigning binding site [J].