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Features of the complex of food additive hesperidin to hemoglobin

Paper ID Volume ID Publish Year Pages File Format Full-Text
30832 44507 2012 8 PDF Available
Title
Features of the complex of food additive hesperidin to hemoglobin
Abstract

The purpose of the current work was to examine the complexation of a mammalian protein, hemoglobin (Hb) with a food additive hesperidin at physiological conditions. Molecular modeling, fluorescence, and circular dichroism (CD) methods were exploited to analyze the binding domain, affinity, and the effects of hesperidin conjugation on Hb spatial structure. From molecular modeling, central cavity of Hb was assigned to retain high-affinity for hesperidin, this corroborates the steady state fluorescence and hydrophobic ANS probe results. The association of hesperidin with Hb emerges fluorescence quenching via static type, this phenomenon display that the ground state complex formation with an affinity of 104 M−1, and hypsochromic effect transpires. Additionally, the alterations of synchronous fluorescence, CD, and three-dimensional fluorescence suggest that the polypeptide chain of Hb partially folding after conjugation with hesperidin. The above data suggest that Hb plays a significant role in the plasma distribution and transportation of hesperidin and related dietary flavonoids.

Graphical abstractHesperidin situates within the central cavity of Hb, as well as the amino acid residues, such as Tyr-35, Trp-37, Pro-95, Phe-98, Lys-99, Glu-101, and Asp-126, which all keep an appropriate distance involved in making hydrogen bonds, π–π, and electrostatic interactions with hesperidin, this conjugation arouses faint folding of the polypeptide chain of protein, ascends the hydrophobicity and leads to structural changes.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Central cavity of Hb is designated to possess high-affinity for hesperidin. ► Static type is dominance for the reduction in the β-37 Trp residue fluorescence. ► Hydrogen bond, π–π, and electrostatic interaction exist between Hb and hesperidin. ► Hb structure folds upon complex with hesperidin. ► Our task disclose flavonoids absorption, bioavailability, and biological activity.

Keywords
Flavonoid; Hesperidin; Hemoglobin; Molecular modeling; Fluorescence; Circular dichroism
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 106, 5 January 2012, Pages 53–60
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us