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Reversible Dimerization of Human Serum Albumin. / Chubarov, Alexey; Spitsyna, Anna; Krumkacheva, Olesya et al.

In: Molecules (Basel, Switzerland), Vol. 26, No. 1, 108, 01.2021.

Research output: Contribution to journal › Article › peer-review

Harvard

Chubarov, A, Spitsyna, A, Krumkacheva, O, Mitin, D, Suvorov, D, Tormyshev, V, Fedin, M, Bowman, MK & Bagryanskaya, E 2021, 'Reversible Dimerization of Human Serum Albumin', Molecules (Basel, Switzerland), vol. 26, no. 1, 108. https://doi.org/10.3390/molecules26010108

APA

Chubarov, A., Spitsyna, A., Krumkacheva, O., Mitin, D., Suvorov, D., Tormyshev, V., Fedin, M., Bowman, M. K., & Bagryanskaya, E. (2021). Reversible Dimerization of Human Serum Albumin. Molecules (Basel, Switzerland), 26(1), [108]. https://doi.org/10.3390/molecules26010108

Vancouver

Chubarov A, Spitsyna A, Krumkacheva O, Mitin D, Suvorov D, Tormyshev V et al. Reversible Dimerization of Human Serum Albumin. Molecules (Basel, Switzerland). 2021 Jan;26(1):108. doi: 10.3390/molecules26010108

Author

Chubarov, Alexey ; Spitsyna, Anna ; Krumkacheva, Olesya et al. / Reversible Dimerization of Human Serum Albumin. In: Molecules (Basel, Switzerland). 2021 ; Vol. 26, No. 1.

BibTeX

@article{50afc7cafc5948329f89012d5983633e,
title = "Reversible Dimerization of Human Serum Albumin",
abstract = "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.",
keywords = "aggregation, human serum albumin, pulse dipole EPR, DIMER, DYNAMICS, BINDING",
author = "Alexey Chubarov and Anna Spitsyna and Olesya Krumkacheva and Dmitry Mitin and Daniil Suvorov and Victor Tormyshev and Matvey Fedin and Bowman, {Michael K.} and Elena Bagryanskaya",
note = "Publisher Copyright: Copyright: {\textcopyright} 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Copyright: Copyright 2021 Elsevier B.V., All rights reserved.",
year = "2021",
month = jan,
doi = "10.3390/molecules26010108",
language = "English",
volume = "26",
journal = "Molecules",
issn = "1420-3049",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "1",

}

RIS

TY - JOUR

T1 - Reversible Dimerization of Human Serum Albumin

AU - Chubarov, Alexey

AU - Spitsyna, Anna

AU - Krumkacheva, Olesya

AU - Mitin, Dmitry

AU - Suvorov, Daniil

AU - Tormyshev, Victor

AU - Fedin, Matvey

AU - Bowman, Michael K.

AU - Bagryanskaya, Elena

N1 - Publisher Copyright: Copyright: © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Copyright: Copyright 2021 Elsevier B.V., All rights reserved.

PY - 2021/1

Y1 - 2021/1

N2 - 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.

AB - 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.

KW - aggregation

KW - human serum albumin

KW - pulse dipole EPR

KW - DIMER

KW - DYNAMICS

KW - BINDING

UR - http://www.scopus.com/inward/record.url?scp=85099176329&partnerID=8YFLogxK

U2 - 10.3390/molecules26010108

DO - 10.3390/molecules26010108

M3 - Article

C2 - 33383640

AN - SCOPUS:85099176329

VL - 26

JO - Molecules

JF - Molecules

SN - 1420-3049

IS - 1

M1 - 108

ER -

ID: 27449118