The use of heated capillary dissociation and collision-induced dissociation to determine the strength of noncovalent bonding interactions in gas-phase peptide-cyclodextrin complexes

Sharron G. Penn, Fei He, M. Kirk Green, Carlito B Lebrilla

Research output: Contribution to journalArticle

55 Scopus citations

Abstract

Complexes of four peptides and permethylated-β-cyclodextrin are produced in the gas phase by using electrospray ionization. The four peptides-bradykinin (BK), des-Arg-1 bradykinin (dR1BK), des-Arg-9-bradykinin (dR9BK), and Gly-5-Gly-8-bradykinin (G5G8BK)-were chosen because the relative inclusion and protonation sites varied with each peptide. Collision induced dissociation (CID) was performed to determine the dissociation threshold of the four complexes. Heated capillary dissociation (HCD) was used to determine the dissociation temperatures of the peptide complexes. CID and HCD indicate the same ordering of stability in the complexation of the peptides to the oligosaccharides. Increasing strength of interaction follows the order dR9BK < BK < dR1BK ≃ G5G8BK. The absence of Arg-9 destabilizes the complex, whereas the absence of Arg-1 stabilizes it relative to BK. Replacing both Phe residues with Gly similarly strengthens the interaction, suggesting that the Phe destabilizes the complex. CID and HCD are useful methods for obtaining relative strengths of interaction in noncovalent bound complexes.

Original languageEnglish (US)
Pages (from-to)244-252
Number of pages9
JournalJournal of the American Society for Mass Spectrometry
Volume8
Issue number3
DOIs
StatePublished - Mar 1997

ASJC Scopus subject areas

  • Structural Biology
  • Spectroscopy

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