Reversible Dimerization of Human Serum Albumin

Reversible Dimerization of Human Serum Albumin Full article

Journal

Molecules
, E-ISSN: 1420-3049

Output data

Year: 2021, Volume: 26, Number: 1, Article number : 108, Pages count : DOI: 10.3390/molecules26010108

Tags

human serum albumin; pulse dipole EPR; aggregation

Authors

Chubarov Alexey ^1,2 , Spitsyna Anna ^2,3 , Krumkacheva Olesya ^2,4 , Mitin Dmitry ^1,2 , Suvorov Daniil ^1,2 , Tormyshev Victor ⁴ , Fedin Matvey ^2,4 , Bowman Michael K. ^4,5 , Bagryanskaya Elena ⁴

Affiliations

1	Institute of Chemical Biology and Fundamental Medicine SB RAS, 630090 Novosibirsk, Russia
2	Novosibirsk State University, 630090 Novosibirsk, Russia
3	N.N. Vorozhtsov Institute of Organic Chemistry SB RAS, 630090 Novosibirsk, Russia
4	International Tomography Center SB RAS, 630090 Novosibirsk, Russia
5	Department of Chemistry & Biochemistry, University of Alabama, Tuscaloosa, AL 35487, USA

Pulsed Dipolar Spectroscopy (PDS) methods of Electron Paramagnetic Resonance (EPR) were used to detect and characterize reversible non-covalent dimers of Human Serum Albumin (HSA), the most abundant protein in human plasma. The spin labels, MTSL and OX063, were attached to Cys-34 and these chemical modifications of Cys-34 did affect the dimerization of HSA, indicating that other post-translational modifications can modulate dimer formation. At physiologically relevant concentrations, HSA does form weak, non-covalent dimers with a well-defined structure. Dimer formation is readily reversible into monomers. Dimerization is very relevant to the role of HSA in the transport, binding, and other physiological processes.

Chubarov A. , Spitsyna A. , Krumkacheva O. , Mitin D. , Suvorov D. , Tormyshev V. , Fedin M. , Bowman M.K. , Bagryanskaya E.
Reversible Dimerization of Human Serum Albumin

Molecules. 2021. V.26. N1. 108 . DOI: 10.3390/molecules26010108 WOS Scopus

Full text from publisher

Published online:

Dec 29, 2020

Web of science	WOS:000606042300001
Scopus	2-s2.0-85099176329
OpenAlex	W3117876055