Role of the Cysteine in R3 Tau Peptide in Copper Binding and Reactivity.
Alzheimer’s disease
copper complexes
cysteine oxidation
oxidative stress
post-translational protein modification
tau protein
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
14 Sep 2022
14 Sep 2022
Historique:
received:
26
07
2022
revised:
07
09
2022
accepted:
10
09
2022
entrez:
23
9
2022
pubmed:
24
9
2022
medline:
28
9
2022
Statut:
epublish
Résumé
Tau is a widespread neuroprotein that regulates the cytoskeleton assembly. In some neurological disorders, known as tauopathies, tau is dissociated from the microtubule and forms insoluble neurofibrillary tangles. Tau comprises four pseudorepeats (R1-R4), containing one (R1, R2, R4) or two (R3) histidines, that potentially act as metal binding sites. Moreover, Cys291 and Cys322 in R2 and R3, respectively, might have an important role in protein aggregation, through possible disulfide bond formation, and/or affecting the binding and reactivity of redox-active metal ions, as copper. We, therefore, compare the interaction of copper with octadeca-R3-peptide (R3C) and with the mutant containing an alanine residue (R3A) to assess the role of thiol group. Spectrophotometric titrations allow to calculate the formation constant of the copper(I) complexes, showing a remarkable stronger interaction in the case of R3C (log
Identifiants
pubmed: 36142637
pii: ijms231810726
doi: 10.3390/ijms231810726
pmc: PMC9503722
pii:
doi:
Substances chimiques
Disulfides
0
Peptides
0
Protein Aggregates
0
tau Proteins
0
Copper
789U1901C5
Cysteine
K848JZ4886
Alanine
OF5P57N2ZX
Dopamine
VTD58H1Z2X
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Ministry of Education, Universities and Research
ID : 2015T778JW
Organisme : COST
ID : CA18202
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