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Positional preferences in flavonoids for inhibition of ribonuclease A: Where ' <scp>OH</scp> ' where?
- Source :
- Proteins: Structure, Function, and Bioinformatics. 89:577-587
- Publication Year :
- 2021
- Publisher :
- Wiley, 2021.
-
Abstract
- Flavonoids are a class of polyphenols that possess diverse properties. The structure-activity relationship of certain flavonoids and resveratrol with ribonuclease A (RNase A) has been investigated. The selected flavonoids have a similar skeleton and the positional preferences of the phenolic moieties toward inhibition of the catalytic activity of RNase A have been studied. The results obtained for RNase A inhibition by flavonoids suggest that the planarity of the molecules is necessary for effective inhibitory potency. Agarose gel electrophoresis and precipitation assay experiments along with kinetic studies reveal Ki values for the various flavonoids in the micromolar range. Minor secondary structural changes of RNase A were observed after interaction with the flavonoids. An insight into the specific amino acid involvement in the binding of the substrate using docking studies is also presented. The dipole moment of the flavonoids that depends on the orientation of the hydroxyl groups in the molecule bears direct correlation with the inhibitory potency against RNase A. The direct association of this molecular property with enzyme inhibition can be exploited for the design and development of inhibitors of proteins.
- Subjects :
- Models, Molecular
Protein Conformation, alpha-Helical
Flavonols
RNase P
Biochemistry
Substrate Specificity
03 medical and health sciences
Structural Biology
Catalytic Domain
Molecular property
Animals
Protein Interaction Domains and Motifs
heterocyclic compounds
Ribonuclease
Enzyme Inhibitors
Kaempferols
Pancreas
Molecular Biology
030304 developmental biology
Flavonoids
chemistry.chemical_classification
0303 health sciences
biology
Chemistry
fungi
030302 biochemistry & molecular biology
food and beverages
Substrate (chemistry)
Ribonuclease, Pancreatic
Protein Structure, Tertiary
Amino acid
carbohydrates (lipids)
Kinetics
Resveratrol
Docking (molecular)
Polyphenol
Flavanones
Agarose gel electrophoresis
biology.protein
Thermodynamics
Cattle
Protein Conformation, beta-Strand
Quercetin
Protein Binding
Subjects
Details
- ISSN :
- 10970134 and 08873585
- Volume :
- 89
- Database :
- OpenAIRE
- Journal :
- Proteins: Structure, Function, and Bioinformatics
- Accession number :
- edsair.doi.dedup.....92cca6300fdffd7b7962e3e7f177bc93