Determination of Relative Stabilities of Metal-Peptide Bonds in the Gas Phase.

ABSTRACT: Understanding binding site preferences in biological systems as well as affinities to binding partners is a crucial aspect in metallodrug development. We here present a mass spectrometry-based method to compare relative stabilities of metal-peptide adducts in the gas phase. Angiotensin 1 and substance P were used as model peptides. Incubation with isostructural N-heterocyclic carbene (NHC) complexes of Ru^II , Os^II , Rh^III , and Ir^III led to the formation of various adducts, which were subsequently studied by energy-resolved fragmentation experiments. The gas-phase stability of the metal-peptide bonds depended on the metal and the binding partner. Of the four complexes used, the Os^II derivative bound strongest to Met, while Ru^II

SUBMITTER: Cziferszky M 

PROVIDER: S-EPMC9298285 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature