Local dynamics analysis of human insulin and a rapid- acting insulin analog by hydrogen deuterium exchange/mass spectrometry

摘要

1. The deuteration levels of lispro peptides were different from those of human insulin peptides. This result agrees with the previous results of intact HDX. 2. We determined two particular regions, chain A1 -4 and chain B22-24, which exhibited higher deuterium uptake in lispro. Importantly, chain A1-4 and chain B22-24 were expected to be involved in hexamerization and dimerization, respectively. 3. HDX study enables to probe the difference in dissociative events of insulin oligomers, and the results are useful to understand their dissociation.