The unusual properties of lactoferrin during its nascent phase.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
29 08 2023
29 08 2023
Historique:
received:
18
05
2023
accepted:
21
08
2023
medline:
31
8
2023
pubmed:
30
8
2023
entrez:
29
8
2023
Statut:
epublish
Résumé
Lactoferrin, a multifunctional iron-binding protein containing 16 disulfides, is actively studied for its antibacterial and anti-carcinogenic properties. However, scarce information is nowadays available about its oxidative folding starting from the reduced and unfolded status. This study discovers unusual properties when this protein is examined in its reduced molten globule-like conformation. Using kinetic, CD and fluorescence analyses together with mass spectrometry, we found that a few cysteines display astonishing hyper-reactivity toward different thiol reagents. In details, four cysteines (i.e. 668, 64, 512 and 424) display thousands of times higher reactivity toward GSSG but normal against other natural disulfides. The formation of these four mixed-disulfides with glutathione probably represents the first step of its folding in vivo. A widespread low pK
Identifiants
pubmed: 37644064
doi: 10.1038/s41598-023-41064-x
pii: 10.1038/s41598-023-41064-x
pmc: PMC10465537
doi:
Substances chimiques
Glutathione Disulfide
ULW86O013H
Lactoferrin
EC 3.4.21.-
Albumins
0
Anti-Bacterial Agents
0
Cysteine
K848JZ4886
Disulfides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
14113Informations de copyright
© 2023. Springer Nature Limited.
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