Chemical synthesis of per‐selenocysteine human epidermal growth factor. (19th December 2022)

• Record Type: Journal Article
• Authors: Takei, Toshiki; Tanaka, Hideaki; Okumura, Nobuaki; Takao, Toshifumi; Moroder, Luis; Hojo, Hironobu
• Is Part Of: Journal of peptide science. Volume 29:Number 5(2023)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2022-12-19
• Subjects: Cys‐to‐Sec substitution -- enhanced stability to reduction -- epidermal growth factor -- oxidative folding -- selenocysteine; Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.3464
• Languages: English
• ISSNs: 1075-2617

Abstract

Abstract : 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. Abstract : Selenocysteine (Sec)‐substituted epidermal growth factor (seleno‐EGF), in which all cysteine residues of human EGF are replaced by Sec, was synthesized. After folding, the seleno‐EGF showed a comparable structure and biological activity with that of native EGF. Unlike human EGF, it is stable under reducing conditions, making Cys‐to‐Sec substitution an efficient method to create more stable bioactive peptides.