| Cross-talk between amino acid residues and flavonoid derivatives: insights into their chemical recognition. | |
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MedLine Citation:
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PMID: 23086511 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Currently, there is a general consensus that flavonoids exert their antioxidant activity through their ability to interact with a broad range of proteins, enzymes and transcription factors rather than acting as conventional hydrogen-donating antioxidants. For this, the effect of different chemical groups of the conjugated flavonoid metabolites is apparently playing a pivotal role. Yet, many questions concerning the relevant molecular mechanisms still remain open. It is therefore crucial to gain a deeper insight into the amino acid residue-flavonoid interaction. Here we show extensive theoretical thermodynamic data and structural characteristics of the interaction of chalcone, genistein, epigallocatechin gallate, and quercetin and some of its metabolites with amino acid residues. By correlating (a) the binding energies of flavonoids-amino acid residues, (b) the hydrophobicity of amino acids, and (c) the abundance of amino acid residues in the binding sites of proteins, we can conclude that flavonoids appear to be strongly bonded to only few charged hydrophilic amino acids in the protein pockets, and rather weakly bonded to the majority of amino acid residues in the binding sites. This finding strongly impacts the understanding of the chemical recognition of flavonoids and their metabolites in their interaction with proteins and would contribute to a better design of further experimental studies. Particularly, the amino acids Phe, Leu, Ile and Trp seem to play a crucial role in the dynamics of flavonoid ligands in the binding sites of proteins. |
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Authors:
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A Daniel Boese; Edelsys Codorniu-Hernández |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-10-19 |
Journal Detail:
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Title: Physical chemistry chemical physics : PCCP Volume: - ISSN: 1463-9084 ISO Abbreviation: Phys Chem Chem Phys Publication Date: 2012 Oct |
Date Detail:
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Created Date: 2012-10-22 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 100888160 Medline TA: Phys Chem Chem Phys Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Department of Chemistry, Humboldt-Universität zu Berlin, Unter den Linden 6, 10099 Berlin, Germany. daniel.boese@chemie.hu-berlin.de. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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