Collected Item: “Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?”
Врста публикације
Рад у часопису
Верзија рада
објављена верзија
Језик рада
енглески
Аутор/и (Милан Марковић, Никола Николић)
Lena Platanić Arizanović, Nikola Gligorijević, Ilija Cvijetić, Aleksandar Mijatović, Maja Krstić Ristivojević, Simeon Minić, Aleksandra Nikolić Kokić, Čedo Miljević, Milan Nikolić
Наслов рада (Наслов - поднаслов)
Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?
Наслов часописа
International Journal of Molecular Sciences
Издавач (Београд : Просвета)
MDPI AG
Година издавања
2023
Сажетак на енглеском језику
Packed with hemoglobin, an essential protein for oxygen transport, human erythrocytes are a suitable model system for testing the pleiotropic effects of lipophilic drugs. Our study investigated the interaction between antipsychotic drugs clozapine, ziprasidone, sertindole, and human hemoglobin under simulated physiological conditions. Analysis of protein fluorescence quenching
at different temperatures and data obtained from the van’t Hoff diagram and molecular docking indicate that the interactions are static and that the tetrameric human hemoglobin has one binding site for all drugs in the central cavity near αβ interfaces and is dominantly mediated through hydrophobic forces. The association constants were lower-moderate strength (~104 M−1
), the highest observed for clozapine (2.2 × 104 M−1 at 25 ◦C). The clozapine binding showed “friendly” effects: increased α-helical content, a higher melting point, and protein protection from free radical-mediated oxidation. On the other hand, bound ziprasidone and sertindole had a slightly pro-oxidative effect, increasing ferrihemoglobin content, a possible “foe”. Since the interaction of proteins with drugs plays a vital role in their pharmacokinetic and pharmacodynamic properties, the physiological significance of the obtained findings is briefly discussed.
at different temperatures and data obtained from the van’t Hoff diagram and molecular docking indicate that the interactions are static and that the tetrameric human hemoglobin has one binding site for all drugs in the central cavity near αβ interfaces and is dominantly mediated through hydrophobic forces. The association constants were lower-moderate strength (~104 M−1
), the highest observed for clozapine (2.2 × 104 M−1 at 25 ◦C). The clozapine binding showed “friendly” effects: increased α-helical content, a higher melting point, and protein protection from free radical-mediated oxidation. On the other hand, bound ziprasidone and sertindole had a slightly pro-oxidative effect, increasing ferrihemoglobin content, a possible “foe”. Since the interaction of proteins with drugs plays a vital role in their pharmacokinetic and pharmacodynamic properties, the physiological significance of the obtained findings is briefly discussed.
Волумен/том или годиште часописа
24
Број часописа
10
DOI број
10.3390/ijms24108921
ISSN број часописа
1422-0067
Кључне речи на српском (одвојене знаком ", ")
Inorganic Chemistry,Organic Chemistry,Physical and Theoretical Chemistry,Computer Science Applications,Spectroscopy,Molecular Biology,General Medicine,Catalysis
Кључне речи на енглеском (одвојене знаком ", ")
Inorganic Chemistry,Organic Chemistry,Physical and Theoretical Chemistry,Computer Science Applications,Spectroscopy,Molecular Biology,General Medicine,Catalysis
Линк
https://www.mdpi.com/1422-0067/24/10/8921/pdf
Шира категорија рада према правилнику МПНТ
M20
Ужа категорија рада према правилнику МПНТ
М21
Степен доступности
Затворени приступ
Лиценца
Creative Commons – Attribution-No Derivative Works 4.0 International
Формат дигиталног објекта
.pdf