In(III) pyridinecarboxylate complexes: Composition, solution equilibria estimation, bioevaluation and interactions with HSA

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F25%3A00598450" target="_blank" >RIV/61388955:_____/25:00598450 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/25:10489288

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0162013424002629?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0162013424002629?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jinorgbio.2024.112738" target="_blank" >10.1016/j.jinorgbio.2024.112738</a>

Jazyk výsledku

angličtina

Název v původním jazyce

In(III) pyridinecarboxylate complexes: Composition, solution equilibria estimation, bioevaluation and interactions with HSA

Popis výsledku v původním jazyce

Two In(III) – pyridinecarboxylates ([In(Pic)2(NO3)(H2O)] (InPic, HPic = picolinic acid), [In(HDpic)(Dpic)(H2O)2]·5H2O (InDpic, H2Dpic = dipicolinic acid), have been synthesized by one-step procedure. The complexes composition was confirmed by physicochemical analyses and X-ray diffraction confirmed molecular structure of both complexes. Moreover, complex species speciation was described in both systems by potentiometry and 1H NMR spectroscopy and mononuclear complex species were determined, [In(Pic)]2+ (logβ011 = 6.94(4)), [In(Pic)2]+ (logβ021 = 11.98(9)), [In(Dpic)]+ (logβ011 = 10.42(6)), [In(Dpic)2]− (logβ021 = 17.58(7)) and [In(Dpic)2(OH)]2− (logβ−121 = 10.18(6)). To confirm the complexes stability in 1 % DMSO, 1H NMR spectra were measured (immediately after dissolution up to 96 h). Antimicrobial and anticancer assays indicate a more significant sensitivity of S. aureus bacteria and MDA-MB-231 cancer cells to the InPic complex (IC50 = 25 and 340.7 μM) than to the InDpic (IC50 = 50 and 975.4 μM). The interaction and binding mechanism of picolinic/dipicolinic acid and their indium(III) complexes with HSA (human serum albumin) were studied using fluorescence and CD spectroscopy. The results confirmed that the studied compounds had bound successfully to HSA, and the binding parameters and constants (KSV, Kq, Kb) were calculated together with the number of binding sites. The binding forces were identified based on calculated thermodynamic parameters (ΔG, ΔH, ΔS). Synchronous spectra were used to study the microenvironment of Tyr and Trp residues and displacement assays revealed that site I was the preferred binding site. After binding, conformational changes were found to have occurred in the HSA molecule and the % α-helical content had decreased.

Název v anglickém jazyce

In(III) pyridinecarboxylate complexes: Composition, solution equilibria estimation, bioevaluation and interactions with HSA

Popis výsledku anglicky

Two In(III) – pyridinecarboxylates ([In(Pic)2(NO3)(H2O)] (InPic, HPic = picolinic acid), [In(HDpic)(Dpic)(H2O)2]·5H2O (InDpic, H2Dpic = dipicolinic acid), have been synthesized by one-step procedure. The complexes composition was confirmed by physicochemical analyses and X-ray diffraction confirmed molecular structure of both complexes. Moreover, complex species speciation was described in both systems by potentiometry and 1H NMR spectroscopy and mononuclear complex species were determined, [In(Pic)]2+ (logβ011 = 6.94(4)), [In(Pic)2]+ (logβ021 = 11.98(9)), [In(Dpic)]+ (logβ011 = 10.42(6)), [In(Dpic)2]− (logβ021 = 17.58(7)) and [In(Dpic)2(OH)]2− (logβ−121 = 10.18(6)). To confirm the complexes stability in 1 % DMSO, 1H NMR spectra were measured (immediately after dissolution up to 96 h). Antimicrobial and anticancer assays indicate a more significant sensitivity of S. aureus bacteria and MDA-MB-231 cancer cells to the InPic complex (IC50 = 25 and 340.7 μM) than to the InDpic (IC50 = 50 and 975.4 μM). The interaction and binding mechanism of picolinic/dipicolinic acid and their indium(III) complexes with HSA (human serum albumin) were studied using fluorescence and CD spectroscopy. The results confirmed that the studied compounds had bound successfully to HSA, and the binding parameters and constants (KSV, Kq, Kb) were calculated together with the number of binding sites. The binding forces were identified based on calculated thermodynamic parameters (ΔG, ΔH, ΔS). Synchronous spectra were used to study the microenvironment of Tyr and Trp residues and displacement assays revealed that site I was the preferred binding site. After binding, conformational changes were found to have occurred in the HSA molecule and the % α-helical content had decreased.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2025

Kód důvěrnosti údajů

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

Název periodika

Journal of Inorganic Biochemistry

ISSN

0162-0134

e-ISSN

1873-3344

Svazek periodika

262

Číslo periodika v rámci svazku

JAN 2025

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

17

Strana od-do

112738

Kód UT WoS článku

001318124800001

EID výsledku v databázi Scopus

2-s2.0-85203831797