Conformationally Regulated Peptide Bond Cleavage in Bradykinin.

ABSTRACT: Ion mobility and mass spectrometry techniques are used to investigate the stabilities of different conformations of bradykinin (BK, Arg¹-Pro²-Pro³-Gly⁴-Phe⁵-Ser⁶-Pro⁷-Phe⁸-Arg⁹). At elevated solution temperatures, we observe a slow protonation reaction, i.e., [BK+2H]²⁺+H⁺ → [BK+3H]³⁺, that is regulated by trans → cis isomerization of Arg¹-Pro², resulting in the Arg¹- cis-Pro²- cis-Pro³-Gly⁴-Phe⁵-Ser⁶- cis-Pro⁷-Phe⁸-Arg⁹ (all- cis) configuration. Once formed, the all- cis [BK+3H]³⁺ spontaneously cleaves the bond between Pro^2</

SUBMITTER: Fuller DR 

PROVIDER: S-EPMC6503673 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature