The effects of biliverdin on pressure-induced unfolding of apomyoglobin: The specific role of Zn
Apomyoglobin
Biliverdin
Binding
High-pressure
Stability
Zinc
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
01 Aug 2023
01 Aug 2023
Historique:
received:
24
02
2023
revised:
05
06
2023
accepted:
22
06
2023
medline:
2
8
2023
pubmed:
26
6
2023
entrez:
25
6
2023
Statut:
ppublish
Résumé
Apomyoglobin (apoMb), a model protein in biochemistry, exhibits a strong propensity to bind various ligands, which makes it a good candidate as a carrier of bioactive hydrophobic drugs. The stability of its hydrophobic pocket determines its potential as a carrier of bioactive compounds. High pressure (HP) is a potent tool for studying protein stability, revealing the specific role of hydrophobic cavities in unfolding. We probed the effects of biliverdin (BV) binding and its complex with Zn
Identifiants
pubmed: 37356686
pii: S0141-8130(23)02443-1
doi: 10.1016/j.ijbiomac.2023.125549
pii:
doi:
Substances chimiques
apomyoglobin
0
Biliverdine
O9MIA842K9
Myoglobin
0
Apoproteins
0
Ions
0
Zinc
J41CSQ7QDS
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
125549Informations de copyright
Copyright © 2023. Published by Elsevier B.V.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.