Abstract
Formation of chiral amyloid superstructures is a newly recognised phenomenon observed upon agitation-assisted fibrillation of bovine insulin. Here, by surveying several amyloidogenic precursors we examine whether formation of such entities is unique to bovine insulin. Our results indicate that only bovine, human, and porcine insulins are capable of chiral superstructural self-assembly. A tiny covalent perturbation consisting in reversal of ProB28-LysB29 residues in a human insulin analog is sufficient to prevent this process. Our study suggests that insulin’s dimer-forming interface – specifically the B-chain’s C-terminal fragment – may acquire the new role of a molecular velcro upon lateral alignment of individual fibrils into superstructures. Structured summary of protein interactionsBI and BIbind by infrared spectroscopy (View interaction)HI and HIbind by atomic force microscopy (View interaction)HEWL and HEWLbind by circular dichroism (View interaction)BI and BIbind by circular dichroism (View interaction)α-LAC and α-LACbind by circular dichroism (View interaction)BI and BIbind by atomic force microscopy (View interaction)α-LAC and α-LACbind by atomic force microscopy (View interaction)HI and HIbind by circular dichroism (View interaction)PI and PIbind by circular dichroism (View interaction)PI and PIbind by atomic force microscopy (View interaction)HEWL and HEWLbind by atomic force microscopy (View interaction)
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