Binding constants and in silico analysis of albumin interaction with phenolic acids and flavonoids

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00027006%3A_____%2F24%3A10177162" target="_blank" >RIV/00027006:_____/24:10177162 - isvavai.cz</a>

Result on the web

<a href="https://hemija.pmf.unsa.ba/glasnik/files/Issue%2062/5_13-24_Topcagic1.pdf" target="_blank" >https://hemija.pmf.unsa.ba/glasnik/files/Issue%2062/5_13-24_Topcagic1.pdf</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.35666/2232-7266.2024.62.03" target="_blank" >10.35666/2232-7266.2024.62.03</a>

Result language

angličtina

Original language name

Binding constants and in silico analysis of albumin interaction with phenolic acids and flavonoids

Original language description

In this study, fluorescence techniques were utilized to investigate the interactions of selected phenolic acids (PAs) and flavonoids (FLs) with bovine serum albumin (BSA) under physiological conditions. The binding of PAs/FLs with BSA was investigated at three temperatures: 292, 303 and 310 K. From the obtained spectra, the Stern-Volmer constant ( K sv ), bimolecular quenching constant ( k q ), binding constants ( K b ), and binding site number ( n ) constants were calculated. Presented results indicate that fluorescence quenching of BSA in the presence of phenolic acids/flavonoids is a static quenching process. The strongest static binding occurs during the formation of the BSA-pHBA ( p-hydroxybenzoic acid) complex ( k q = 57.1x10 12 M-1 s-1 at 292 K), and BSA-Que (quercetin) complex ( k q = 42.8x10 12 M-1 s-1 at 292 K). The structure of PAs/FLs was revealed to significantly affect the binding/quenching process and additionaly, fluorescence resonance energy transfer studies confirmed the static nature of this process. The results of synchronous fluorescence spectra suggest changes in the microenvironment of tyrosine. Three-dimensional spectra showed changes related to the backbone structures of the protein chain (caused by the pi- pi &amp; lowast; transition of the carbonyl group). Furthermore, thermal denaturation was performed by nano differential scanning fluorimetry (nanoDSF) and transition temperature ( T m ) values for BSA complexes with PAs/FLs are slightly lower than T m for BSA, except T m for BSA complexes with kaempferol and chrysine. According to in silico analysis, theoretically, caffeic acid and quercetin showed the best binding position with albumin (4F5S).

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

40106 - Agronomy, plant breeding and plant protection; (Agricultural biotechnology to be 4.4)

Project

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Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2024

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

GLASNIK HEMICARA I TEHNOLOGA BOSNE I HERCEGOVINE

ISSN

0367-4444

e-ISSN

2232-7266

Volume of the periodical

62

Issue of the periodical within the volume

JUN 2024

Country of publishing house

BA - BOSNIA AND HERZEGOVINA

Number of pages

12

Pages from-to

13-24

UT code for WoS article

001270049600003

EID of the result in the Scopus database

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