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Pregled bibliografske jedinice broj: 1150495

Analysis of binding affinity between antiplatelet drug dipyridamole and human serum alpha-1 acid glycoprotein utilizing microscale thermophoresis


Kerep, Robert; Šeba, Tino; Gabričević, Mario
Analysis of binding affinity between antiplatelet drug dipyridamole and human serum alpha-1 acid glycoprotein utilizing microscale thermophoresis // 8th EFMC Young Medicinal Chemists’ Symposium
Basel, Švicarska, 2021. str. 119-119 (poster, međunarodna recenzija, kratko priopćenje, znanstveni)


CROSBI ID: 1150495 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Analysis of binding affinity between antiplatelet drug dipyridamole and human serum alpha-1 acid glycoprotein utilizing microscale thermophoresis

Autori
Kerep, Robert ; Šeba, Tino ; Gabričević, Mario

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, kratko priopćenje, znanstveni

Izvornik
8th EFMC Young Medicinal Chemists’ Symposium / - , 2021, 119-119

Skup
8th EFMC Young Medicinal Chemists’ Symposium

Mjesto i datum
Basel, Švicarska, 09-10.09.2021

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
alpha-acid glycoprotein, plasma protein binding, dipyridamole, binding constant, thermophoresis

Sažetak
An understanding of the interaction of various drugs with plasma proteins is essential for understanding their systemic pharmacology and toxicology. Thus, information concerning the effects of the acute phase responses on the ligand binding ability of plasma can be used to optimize drug administration protocols in clinical practice. Alpha-1 acid glycoprotein (AGP) has been reported to be a major plasma protein that strongly binds basic drugs such as dipyridamole, drug that is easily synthesized from 5-nitroorotic acid (1-2). In this study, microscale thermophoresis (MST) is used as an analytical technique for determining binding affinity between antiplatelet drug dipyridamole and AGP. MST is a powerful technique in quantitation of binding events based on the movement of molecules in microscopic temperature gradient. The concentration of AGP in plasma can significantly increase in various diseases (cancer, inflammatory disease) or following trauma (burns, surgery). Changes in AGP concentration could potentially alter the free fraction of drugs in plasma or at their target sites and eventually affect their pharmacokinetic disposition and pharmacological action. Given that an increase number of drugs have been shown to bind preferentially to AGP, a better understanding of this unique interaction may provide great benefit for drug discovery and development (3). Knowing the change in drug binding affinity to AGP as well as knowing the change in different medical situations can improve the therapeutic and/or toxicological outcome of treatment in dealing with a large number of different drugs.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Farmacija



POVEZANOST RADA


Projekti:
IP-2016-06-3672 - Glikozilacija alfa kiselog glikoproteina - put prema personaliziranoj terapiji (GlycoDrugs) (Gabričević, Mario, HRZZ - 2016-06) ( CroRIS)

Ustanove:
Farmaceutsko-biokemijski fakultet, Zagreb

Profili:

Avatar Url Mario Gabričević (autor)

Avatar Url Tino Šeba (autor)

Avatar Url Robert Kerep (autor)


Citiraj ovu publikaciju:

Kerep, Robert; Šeba, Tino; Gabričević, Mario
Analysis of binding affinity between antiplatelet drug dipyridamole and human serum alpha-1 acid glycoprotein utilizing microscale thermophoresis // 8th EFMC Young Medicinal Chemists’ Symposium
Basel, Švicarska, 2021. str. 119-119 (poster, međunarodna recenzija, kratko priopćenje, znanstveni)
Kerep, R., Šeba, T. & Gabričević, M. (2021) Analysis of binding affinity between antiplatelet drug dipyridamole and human serum alpha-1 acid glycoprotein utilizing microscale thermophoresis. U: 8th EFMC Young Medicinal Chemists’ Symposium.
@article{article, author = {Kerep, Robert and \v{S}eba, Tino and Gabri\v{c}evi\'{c}, Mario}, year = {2021}, pages = {119-119}, keywords = {alpha-acid glycoprotein, plasma protein binding, dipyridamole, binding constant, thermophoresis}, title = {Analysis of binding affinity between antiplatelet drug dipyridamole and human serum alpha-1 acid glycoprotein utilizing microscale thermophoresis}, keyword = {alpha-acid glycoprotein, plasma protein binding, dipyridamole, binding constant, thermophoresis}, publisherplace = {Basel, \v{S}vicarska} }
@article{article, author = {Kerep, Robert and \v{S}eba, Tino and Gabri\v{c}evi\'{c}, Mario}, year = {2021}, pages = {119-119}, keywords = {alpha-acid glycoprotein, plasma protein binding, dipyridamole, binding constant, thermophoresis}, title = {Analysis of binding affinity between antiplatelet drug dipyridamole and human serum alpha-1 acid glycoprotein utilizing microscale thermophoresis}, keyword = {alpha-acid glycoprotein, plasma protein binding, dipyridamole, binding constant, thermophoresis}, publisherplace = {Basel, \v{S}vicarska} }




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