Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Isoquinoline Alkaloids Interaction With Plasma Proteins

Aleksandra Marciniak
ORCID logo ,
Aleksandra Kotynia
ORCID logo ,
Edward Krzyżak
* ORCID logo ,
Żaneta Czyżnikowska
,
Sylwia Zielińska
* ,
Weronika Kozłowska
,
Marcel Białas
,
Adam Matkowski
,
Anna Jezierska-Domaradzka
ORCID logo
Version 1 : Received: 18 April 2024 / Approved: 19 April 2024 / Online: 19 April 2024 (10:26:37 CEST)

How to cite: Marciniak, A.; Kotynia, A.; Krzyżak, E.; Czyżnikowska, Ż.; Zielińska, S.; Kozłowska, W.; Białas, M.; Matkowski, A.; Jezierska-Domaradzka, A. Isoquinoline Alkaloids Interaction With Plasma Proteins. Preprints 2024, 2024041330. https://doi.org/10.20944/preprints202404.1330.v1 Marciniak, A.; Kotynia, A.; Krzyżak, E.; Czyżnikowska, Ż.; Zielińska, S.; Kozłowska, W.; Białas, M.; Matkowski, A.; Jezierska-Domaradzka, A. Isoquinoline Alkaloids Interaction With Plasma Proteins. Preprints 2024, 2024041330. https://doi.org/10.20944/preprints202404.1330.v1

Abstract

A comprehensive study of the interactions of human serum albumin (HSA) and α-1-acid glycoprotein (AAG) with two isoquinoline alkaloids: allocryptopine (ACP) and protopine (PP) was performed. The UV-Vis spectroscopy, molecular docking, competitive binding assays, and circular dichroism (CD) spectroscopy were used for the investigations. The results showed that ACP and PP form spontaneous and stable complexes with HSA and AAG, with ACP displaying a stronger affinity towards both proteins. Molecular docking studies showed also revealed the preferential binding of ACP and PP to specific sites within HSA, with site 2 (IIIA) being identified as the favored location for both alkaloids. This was supported by competitive binding assays using markers specific to HSA's drug binding sites. Similarly, for AAG, a decrease in fluorescence intensity upon addition of the alkaloids to AAG/ Quinaldine Red (QR) complexes indicated the replacement of the marker by the alkaloids, with ACP showing a greater extent of replacement than PP. CD spectroscopy showed that the proteins’ structures remained largely unchanged suggesting that the formation of complexes did not significantly perturb the overall spatial configuration of these macromolecules. These findings are crucial for advancing the knowledge on the natural products-protein interactions and the future design of isoquinoline alkaloid-based therapeutics.

Keywords

protopine; allocryptopine; albumin; orosomucoid; spectroscopy

Subject

Medicine and Pharmacology, Pharmacy

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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