Chemical synthesis of per-selenocysteine human epidermal growth factor.
Cys-to-Sec substitution
enhanced stability to reduction
epidermal growth factor
oxidative folding
selenocysteine
Journal
Journal of peptide science : an official publication of the European Peptide Society
ISSN: 1099-1387
Titre abrégé: J Pept Sci
Pays: England
ID NLM: 9506309
Informations de publication
Date de publication:
May 2023
May 2023
Historique:
revised:
28
11
2022
received:
14
10
2022
accepted:
29
11
2022
medline:
5
4
2023
pubmed:
3
12
2022
entrez:
2
12
2022
Statut:
ppublish
Résumé
Human seleno-epidermal growth factor (seleno-EGF), a 53-residue peptide where all six cysteine residues of the parent human EGF sequence were replaced by selenocysteines, was synthesized and the oxidative folding of a polypeptide containing three diselenide bonds was compared to that of the parent cysteine peptide. The crude high performance liquid chromatography (HPLC) profiles clearly showed that both the native EGF and its selenocysteine-analogue fold smoothly, yielding a single sharp peak, proving that even in the case of three disulfide-bonded polypeptides the disulfide-to-diselenide bond substitution is highly isomorphous, as confirmed by conformational circular dichroism measurements and particularly by the biological assays.
Substances chimiques
Selenocysteine
0CH9049VIS
Cysteine
K848JZ4886
Epidermal Growth Factor
62229-50-9
Peptides
0
Disulfides
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e3464Informations de copyright
© 2022 European Peptide Society and John Wiley & Sons Ltd.
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