Structures and interactions of insulin-like peptides from cone snail venom.

ABSTRACT: The venomous insulin-like peptides released by certain cone snails stimulate hypoglycemic shock to immobilize fish and catch the prey. Compared to human insulin (hIns), the cone snail insulins (Con-Ins) are typically monomeric and shorter in sequence, yet they exhibit moderate hIns-like biological activity. We have modeled six variants of Con-Ins (G3, K1, K2, T1A, T1B, and T2) and carried out explicit-solvent molecular dynamics (MD) simulations of eight types of insulins, two with known structures (hIns and Con-Ins-G1) and six Con-Ins with modeled structures, to characterize key residues of each insulin that interact with the truncated human insulin receptor (μIR). We show that each insulin/μIR complex is stable during explicit-solvent MD simulations and hIns interactions indicate the high

SUBMITTER: Gorai B 

PROVIDER: S-EPMC8816879 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature