Diselenide-bond replacement of the external disulfide bond of insulin increases its oligomerization leading to sustained activity.

ABSTRACT: Seleno-insulin, a class of artificial insulin analogs, in which one of the three disulfide-bonds (S-S's) of wild-type insulin (Ins) is replaced by a diselenide-bond (Se-Se), is attracting attention for its unique chemical and physiological properties that differ from those of Ins. Previously, we pioneered the development of a [C7U^A,C7U^B] analog of bovine pancreatic insulin (SeIns) as the first example, and demonstrated its high resistance against insulin-degrading enzyme (IDE). In this study, the conditions for the synthesis of SeIns via native chain assembly (NCA) were optimized to attain a maximum yield of 72%, which is comparable to the in vitro folding efficiency for single-chain proinsulin. When the resistance of BPIns to IDE was evaluated in the presence of SeIn

SUBMITTER: Arai K 

PROVIDER: S-EPMC10663622 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature