Reversible Dimerization of Human Serum Albumin.
aggregation
human serum albumin
pulse dipole EPR
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
29 Dec 2020
29 Dec 2020
Historique:
received:
11
12
2020
revised:
24
12
2020
accepted:
25
12
2020
entrez:
1
1
2021
pubmed:
2
1
2021
medline:
11
9
2021
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 33383640
pii: molecules26010108
doi: 10.3390/molecules26010108
pmc: PMC7795135
pii:
doi:
Substances chimiques
Spin Labels
0
Cysteine
K848JZ4886
Serum Albumin, Human
ZIF514RVZR
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Russian Foundation for Basic Research
ID : 18-04-00393
Organisme : Ministry of Science and Education of the Russian Federation
ID : 14.W03.31.0034
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