Premium
Peptide polarity and the position of arginine as sources of selectivity during positive electrospray ionisation mass spectrometry
Author(s) -
Abaye Daniel A.,
Pullen Frank S.,
Nielsen Birthe V.
Publication year - 2011
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.5270
Subject(s) - chemistry , peptide , electrospray ionization , mass spectrometry , arginine , electrospray , chromatography , peptide sequence , protein mass spectrometry , amino acid , biochemistry , gene
Electrospray ionisation (ESI) is a selective process and, for similar sized analytes, the intrinsic properties of the molecules affect the ionisation process and their response. This research sets out to determine the effect of some of these properties in peptides: peptide polarity and the presence of arginine at positions 1 and 4 in the amino acid sequence on the ESI response. Six peptides; molecular mass ranges 1.3–1.6 kDa; substance P (SP) and glutamate fibrinopeptide (GFP) and 3.2–3.7 kDa; calcitonin gene‐related peptide (CGRP), vasoactive intestinal peptide (VIP), glucagon‐like peptide 1 (GLP1) and defensin human neutropeptide 2 (DHNP2), were investigated. We have demonstrated that in positive ESI, for similar sized peptides and the same charge state, the responsiveness is in the order: Peptides with N or C terminal arginine > most non‐polar peptides > least non‐polar peptides. Therefore, arginine at the terminal position is a source of selectivity. Data from matrix‐assisted laser desorption ionisation (MALDI) analysis supports that of the ESI experiments: Peptides with a terminal arginine residue generated higher signal intensities. Our observations extend our understanding of the ESI process and provide a rational approach to optimising sensitivity of electrospray conditions where a narrow mass range of peptides are poorly chromatographically resolved. This information will provide for a more effective method development process, especially during label‐free quantitative determination of peptides extracted in solution. Copyright © 2011 John Wiley & Sons, Ltd.