Structural Characterization of Arginine Vasopressin and Lysine Vasopressin by Fourier-Transform Ion Cyclotron Resonance Mass Spectrometry and Infrared Multiphoton Dissociation. Issue 3 (June 2015)

• Record Type: Journal Article
• Authors: Bianco, Giuliana; Battista, Fabio G.; Buchicchio, Alessandro; Amarena, Concetta G.; Schmitt-Kopplin, Philippe; Guerrieri, Antonio
• Is Part Of: European journal of mass spectrometry. Volume 21:Issue 3(2015)
• Page Start: 211
• Page End: 219
• Publication Date: 2015-06
• Subjects: neuropeptides -- arginine-vasopressin -- lysine-vasopressin -- infrared multiphoton dissociation -- liquid chromatography; Mass spectrometry -- Periodicals; Mass Spectrometry; Mass spectrometry; Periodicals; Periodicals; 543.6505
• DOI: 10.1255/ejms.1339
• Languages: English
• ISSNs: 1469-0667

Abstract

Arginine vasopressin (AVP) and lysine vasopressin (LVP) were analyzed by reversed-phase liquid chromatography mass spectrometry using Fourier-transform ion cyclotron resonance (FT-ICR) mass spectrometry (MS) electrospray ionization (ESI) in the positive ion mode. LVP and AVP exhibited the protonated adduct [M + H] + as the predominant ion at m/z 1056.43965 and at m/z 1084.44561, respectively. Infrared multiphoton dissociation (IRMPD), using a CO2 laser source at a wavelength of 10.6 μm, was applied to protonated vasopressin molecules. The IRMPD mass spectra presented abundant mass fragments essential for a complete structural information. Several fragment ions, shared between two target molecules, are discussed in detail. Some previously unpublished fragments were identified unambiguously utilizing the high-resolution and accurate mass information provided by the FT-ICR mass spectrometer. The opening of the disulfide loop and the cleavage of the peptide bonds within the ring were observed even under low-energy fragmentation conditions. Coupling the high-performance FT-ICR mass spectrometer with IRMPD as a contemporary fragmentation technique proved to be very promising for the structural characterization of vasopressin.