Binding of the Bioactive Component Daphnetin to Human Serum Albumin Demonstrated Using Tryptophan Fluorescence Quenching

• Published in: Macromolecular bioscience Vol. 4; no. 5; pp. 520 - 525
• Main Authors: Liu, Jiaqin, Tian, Jianniao, Li, Ying, Yao, Xiaojun, Hu, Zhide, Chen, Xingguo
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 17.05.2004; WILEY‐VCH Verlag; Wiley-VCH
• Subjects: Applied sciences; binding; Biological and medical sciences; Blood. Blood coagulation. Reticuloendothelial system; Circular Dichroism; daphnetin; Exact sciences and technology; Fluorescence; fluorescence quenching; FT-IR; HSA; Humans; Medical sciences; Models, Molecular; Natural polymers; Pharmacology. Drug treatments; Physicochemistry of polymers; Protein Binding; Protein Structure, Tertiary; Proteins; Serum Albumin - chemistry; Serum Albumin - metabolism; Software; Spectroscopy, Fourier Transform Infrared; Temperature; Tryptophan - metabolism; Umbelliferones - chemistry; Umbelliferones - metabolism; Physiological condition; Coumarine derivatives; Temperature effect; Anticoagulant; Serum albumin; Experimental study; Modeling; Protein; Intermolecular interaction; Chinese medicine; Folk medicine; Molecular model; Plant origin; Binding mode; Aqueous solution

Daphnetin (7,8‐dihydroxycoumarin), one of the major bioactive components isolated from Daphne koreane Nakai, has been used in traditional Chinese medicine for the treatment of coagulation disorders. It is also a chelator, an antioxidant and a protein kinase inhibitor. In this paper, a combination of...