NDLI: Studies on the binding of fulvic acid with transferrin by spectroscopic analysis.

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Studies on the binding of fulvic acid with transferrin by spectroscopic analysis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Yang, Guang Zhao, Yan-qin Chen, Lei Chen, Hong-bo Sun, Xiao-ran Dong, Yu Zhang, Xiu-feng
Description	Author Affiliation: Zhang XF ( College of Chemical Engineering, Hebei United University, Tangshan, Hebei 063009, China. Electronic address: xfzhang@iccas.ac.cn.); Yang G ( College of Chemical Engineering, Hebei United University, Tangshan, Hebei 063009, China.); Dong Y ( Department of Literature and Law Tangshan College, Tangshan, Hebei 063000, China.); Zhao YQ ( College of Chemical Engineering, Hebei United University, Tangshan, Hebei 063009, China.); Sun XR ( College of Chemical Engineering, Hebei United University, Tangshan, Hebei 063009, China.); Chen L ( College of Chemical Engineering, Hebei United University, Tangshan, Hebei 063009, China.); Chen HB ( College of Chemical Engineering, Hebei United University, Tangshan, Hebei 063009, China.)
Abstract	Transferrin has shown potential in the delivery of anticancer drugs into primarily proliferating cancer cells that over-express transferrin receptors. Fulvic acid has a wide range of biological and pharmacological activities which caused widespread concerns, the interaction of fulvic acid with human serum transferrin (Tf) has great significance for gaining a deeper insight about anticancer activities of fulvic acid. In this study, the mechanism of interaction between fulvic acid and Tf, has been investigated by using fluorescence quenching, thermodynamics, synchronous fluorescence and circular dichroism (CD) under physiological condition. Our results have shown that fulvic acid binds to Tf and form a new complex, and the calculated apparent association constants are 5.04×10(8) M(-1), 5.48×10(7) M(-1), 7.38×10(6) M(-1) from the fluorescence quenching at 288 K, 298 K, and 310 K. The thermodynamic parameters indicate that hydrogen bonding and weak van der Waals are involved in the interaction between fulvic acid and Tf. The binding of fulvic acid to Tf causes the -helix structure content of the protein to reduce, and resulting that peptide chains of Tf become more stretched. Our results have indicated a mechanism of the interaction between fulvic acid and Tf, which may provide information for possible design of methods to deliver drug molecules via transferrin to target tissues and cells effectively.
ISSN	13861425
Volume Number	137
e-ISSN	18733557
Journal	Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
Language	English
Publisher	Elsevier
Publisher Date	2015-02-25
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Antineoplastic Agents Metabolism Benzopyrans Transferrin Chemistry Binding Sites Circular Dichroism Humans Hydrogen Bonding Models, Molecular Protein Binding Spectrometry, Fluorescence Thermodynamics Journal Article Research Support, Non-u.s. Gov't Discipline Spectroscopy
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Atomic and Molecular Physics, and Optics Analytical Chemistry Instrumentation

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