Gas-phase basicities for ions from bradykinin and its des-arginine analogues

Apparent gas-phase basicities (GB(app)s) for [M + H](+) of bradykinin, des- Arg(1)-bradykinin and des-Arg(9)-bradykinin have been assigned by deprotona tion reactions of [M + 2H](2+) in a Fourier transform ion cyclotron resonan ce mass spectrometer. With a GB(app) of 225.8 +/- 4.2 kcal mol(-1), bradyki nin [M + H](+) is the most basic of the ions studied. Ions from des-Arg(1)- bradykinin and des-Arg9-bradykinin have GB(app) values of 222.8 +/- 4.3 kca l mol(-1) and 214.9 +/- 2.3 kcal mol(-1), respectively. One purpose of this work was to determine a suitable reaction efficiency 'break point' for ass igning GB(app) values to peptide ions using the bracketing method. An effic iency value of 0.1 (i.e. approximately 10% of all collisions resulting in a deprotonation reaction) was used to assign GB(app)s. Support for this crit erion is provided by the fact that our GB(app) values for des-Arg(1)-bradyk inin and des-Arg(9)-bradykinin are identical, within experimental error, to literature values obtained using a modified kinetic method. However, the G B(app)s for bradykinin ions from the two studies differ by 10.3 kcal mol(-1 ). The reason for this is not clear, but may involve conformation differenc es produced by experimental conditions. The results may be influenced by sa lt-bridge conformers and/or by conformational changes caused by the use of a proton-bound heterodimer in the kinetic method. Factors affecting the bas icities of these peptide ions are also discussed, and molecular modeling is used to provide information on protonation sites and conformations. The pr esence of two highly basic arginine residues on bradykinin results in its h igh GB(app), while the basicity of des-Arg(1)-bradykinin ions is increased by the presence of two proline residues at the N-terminus. The proline resi due in the second position folds the peptide chain in a manner that increas es intramolecular hydrogen bonding to the protonated N-terminal amino group of the proline at the first position. Copyright (C) 2001 John Wiley & Sons , Ltd.