Interaction of a Potential Anticancer Agent Hypericin and its Model Compound Emodin with DNA and Bovine Serum Albumin

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F18%3A10379667" target="_blank" >RIV/00216208:11110/18:10379667 - isvavai.cz</a>

Výsledek na webu

<a href="https://doi.org/10.21873/invivo.11347" target="_blank" >https://doi.org/10.21873/invivo.11347</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.21873/invivo.11347" target="_blank" >10.21873/invivo.11347</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Interaction of a Potential Anticancer Agent Hypericin and its Model Compound Emodin with DNA and Bovine Serum Albumin

Popis výsledku v původním jazyce

Background/Aim: We report the incorporation of prospective anticancer agent hypericin into DNA and bovine serum albumin (BSA), respectively, with emphasis on comparison of the differences in interaction mode between hypericin and its model compound emodin. Materials and Methods: Spectrophotometric methods were used for determination of the binding constants of the drug complex with biomacromolecules. Differential scanning calorimetry was applied for evaluation of drug-macromolecule complex thermal stability. Results: The strength of interaction expressed by binding constants was found to be 4.0x10(4) l/mol for hypericin-DNA and 8.1x10(4) l/mol for emodin-DNA complex. Both molecules stabilize bovine serum albumin macromolecule and bind into the hydrophobic cavity in IIA subunit but their localization within the molecule is different. Conclusion: Anticancer agent hypericin and its derivative emodin interact with DNA with medium strength and are probably incorporated into the groove of DNA by hydrogen bonds. Bovine serum albumin can serve as a transport protein for hypericin since the binding force between both molecules is adequate.

Název v anglickém jazyce

Interaction of a Potential Anticancer Agent Hypericin and its Model Compound Emodin with DNA and Bovine Serum Albumin

Popis výsledku anglicky

Background/Aim: We report the incorporation of prospective anticancer agent hypericin into DNA and bovine serum albumin (BSA), respectively, with emphasis on comparison of the differences in interaction mode between hypericin and its model compound emodin. Materials and Methods: Spectrophotometric methods were used for determination of the binding constants of the drug complex with biomacromolecules. Differential scanning calorimetry was applied for evaluation of drug-macromolecule complex thermal stability. Results: The strength of interaction expressed by binding constants was found to be 4.0x10(4) l/mol for hypericin-DNA and 8.1x10(4) l/mol for emodin-DNA complex. Both molecules stabilize bovine serum albumin macromolecule and bind into the hydrophobic cavity in IIA subunit but their localization within the molecule is different. Conclusion: Anticancer agent hypericin and its derivative emodin interact with DNA with medium strength and are probably incorporated into the groove of DNA by hydrogen bonds. Bovine serum albumin can serve as a transport protein for hypericin since the binding force between both molecules is adequate.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

—

Návaznosti

V - Vyzkumna aktivita podporovana z jinych verejnych zdroju

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

In Vivo

ISSN

0258-851X

e-ISSN

—

Svazek periodika

32

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

GR - Řecká republika

Počet stran výsledku

8

Strana od-do

1063-1070

Kód UT WoS článku

000442807900010

EID výsledku v databázi Scopus

2-s2.0-85053040911