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Hydrophilic ester-bearing chlorogenic acid binds to a novel domain to inhibit xanthine oxidase.
Planta Med. 2009 Sep; 75(11):1237-40.PM

Abstract

Caffeic acid is a xanthine oxidase (XO) inhibitor that binds to the molybdopterin region of its active site. Caffeic acid phenethyl ester (CAPE) has higher hydrophobicity and exhibits stronger inhibition potency toward XO. Chlorogenic acid is a quinyl ester of caffeic acid that has increased hydrophilicity and also shows stronger XO inhibitory activity compared with caffeic acid. Caffeic acid and CAPE showed competitive inhibition against XO, whereas chlorogenic acid displayed mixed-type inhibition, implying that it binds to sites other than the active site. Structure-based molecular modeling was performed to account for the different binding characteristics of the hydrophobic and hydrophilic esters of caffeic acid. Chlorogenic acid showed weak binding to the molybdopterin region of XO, while it more strongly bound the flavin adenine dinucleotide region than it did the molybdopterin region. These results provide the basis for interactions of caffeic acid analogues with XO via various binding domains.

Authors+Show Affiliations

Graduate Institute of Medical Sciences, Taipei Medical University, Taipei, Taiwan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19330765

Citation

Wang, Shwu-Huey, et al. "Hydrophilic Ester-bearing Chlorogenic Acid Binds to a Novel Domain to Inhibit Xanthine Oxidase." Planta Medica, vol. 75, no. 11, 2009, pp. 1237-40.
Wang SH, Chen CS, Huang SH, et al. Hydrophilic ester-bearing chlorogenic acid binds to a novel domain to inhibit xanthine oxidase. Planta Med. 2009;75(11):1237-40.
Wang, S. H., Chen, C. S., Huang, S. H., Yu, S. H., Lai, Z. Y., Huang, S. T., & Lin, C. M. (2009). Hydrophilic ester-bearing chlorogenic acid binds to a novel domain to inhibit xanthine oxidase. Planta Medica, 75(11), 1237-40. https://doi.org/10.1055/s-0029-1185521
Wang SH, et al. Hydrophilic Ester-bearing Chlorogenic Acid Binds to a Novel Domain to Inhibit Xanthine Oxidase. Planta Med. 2009;75(11):1237-40. PubMed PMID: 19330765.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Hydrophilic ester-bearing chlorogenic acid binds to a novel domain to inhibit xanthine oxidase. AU - Wang,Shwu-Huey, AU - Chen,Chien-Shu, AU - Huang,Shih-Hao, AU - Yu,Szu-Hsu, AU - Lai,Zhi-Yang, AU - Huang,Sheng-Tung, AU - Lin,Chun-Mao, Y1 - 2009/03/27/ PY - 2009/3/31/entrez PY - 2009/3/31/pubmed PY - 2009/12/16/medline SP - 1237 EP - 40 JF - Planta medica JO - Planta Med VL - 75 IS - 11 N2 - Caffeic acid is a xanthine oxidase (XO) inhibitor that binds to the molybdopterin region of its active site. Caffeic acid phenethyl ester (CAPE) has higher hydrophobicity and exhibits stronger inhibition potency toward XO. Chlorogenic acid is a quinyl ester of caffeic acid that has increased hydrophilicity and also shows stronger XO inhibitory activity compared with caffeic acid. Caffeic acid and CAPE showed competitive inhibition against XO, whereas chlorogenic acid displayed mixed-type inhibition, implying that it binds to sites other than the active site. Structure-based molecular modeling was performed to account for the different binding characteristics of the hydrophobic and hydrophilic esters of caffeic acid. Chlorogenic acid showed weak binding to the molybdopterin region of XO, while it more strongly bound the flavin adenine dinucleotide region than it did the molybdopterin region. These results provide the basis for interactions of caffeic acid analogues with XO via various binding domains. SN - 1439-0221 UR - https://www.unboundmedicine.com/medline/citation/19330765/Hydrophilic_ester_bearing_chlorogenic_acid_binds_to_a_novel_domain_to_inhibit_xanthine_oxidase_ L2 - http://www.thieme-connect.com/DOI/DOI?10.1055/s-0029-1185521 DB - PRIME DP - Unbound Medicine ER -