Abstract:
:Chlorogenic acid (CA) is a well-known ester of caffeic acid present in some food. It is also an active component in traditional Chinese medicines which are used to treat various diseases, but the molecular basis of CA is not clear. In the present work, the proton selective relaxation rate and the affinity index were used to investigate the interaction of CA with human serum albumin and bovine serum albumin under the same buffer conditions. The results indicated that the binding affinity of chlorogenic acid to BSA was stronger than that to HSA. The binding site of the ligand-protein complex was elucidated by molecular docking, and the specific interaction was observed from those hydrogen bonds formed by the ligand and active residues. Using a combination of TR-NOE detection, the optimal ligand conformation was illustrated. Further conformational analysis of the complex revealed that the ability of hydrogen bond formation by polar side chain residues in the binding site of BSA might contribute to the greater binding affinity. The results provide a better understanding of CA binding and should contribute towards the design of modifications of CA for therapeutic purposes.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Wang Y,Zhang T,Xu J,Du Wdoi
10.1016/j.ijbiomac.2010.09.015subject
Has Abstractpub_date
2011-01-01 00:00:00pages
81-6issue
1eissn
0141-8130issn
1879-0003pii
S0141-8130(10)00295-3journal_volume
48pub_type
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