title: Selective covalent bond formation in polypeptide ions via gas-phase ion/ion reaction chemistry.
abstract: Primary amines present in protonated polypeptides can be covalently modified via gas-phase ion/ion reactions using bifunctional reagent ions. The use of reagent anions with a charge-bearing site that leads to strong interactions with the polypeptide, such as sulfonic acid, gives rise to the formation of a long-lived adduct. A distinct reactive functional group, an aldehyde in the present case, can then undergo reaction with the peptide. Collisional activation of the adduct ion formed from a reagent with an aldehyde group and a peptide ion with a primary amine gives rise to water loss in conjunction with imine (Schiff base) formation. The covalently bound modification is retained upon subsequent collisional activation. This work demonstrates the ability to selectively modify polypeptide ions in the gas phase within the context of a multistage mass spectrometry experiment.
authors.affiliation: Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, Indiana 47907-2084, USA.
authors.forename: Hongling
authors.initials: H
authors.lastname: Han
authors.forename: Scott A
authors.initials: SA
authors.lastname: McLuckey
mesh_terms: D000595:Amino Acid Sequence; D000809:Angiotensins / Q000032:analysis; D005740:Gases / Q000737:chemistry; D007477:Ions / Q000032:analysis*; D013058:Mass Spectrometry; D010455:Peptides / Q000032:analysis*; D012545:Schiff Bases / Q000032:analysis
chemical_list: D000809:Angiotensins; D005740:Gases; D007477:Ions; D010455:Peptides; D012545:Schiff Bases
references.citation: Mass Spectrom Rev. 2005 Nov-Dec;24(6):931-58
references.pmid: 15706594
references.citation: Int J Mass Spectrom. 2008 Oct 1;276(2-3):149-152
references.pmid: 19424441
references.citation: J Am Soc Mass Spectrom. 2005 Nov;16(11):1750-6
references.pmid: 16182558
references.citation: J Am Soc Mass Spectrom. 2000 Mar;11(3):244-56
references.pmid: 10697820
references.citation: Proteomics. 2004 Jun;4(6):1684-94
references.pmid: 15174137
references.citation: J Am Chem Soc. 2003 Jul 2;125(26):7756-7
references.pmid: 12822966
references.citation: Anal Chem. 2005 Oct 1;77(19):6300-9
references.pmid: 16194092
references.citation: Mol Cell Proteomics. 2004 Dec;3(12):1154-69
references.pmid: 15385600
references.citation: Nat Biotechnol. 1999 Oct;17(10):994-9
references.pmid: 10504701
references.citation: Anal Chem. 2005 May 15;77(10):3173-82
references.pmid: 15889906
references.citation: Mass Spectrom Rev. 1998 Nov-Dec;17(6):369-407
references.pmid: 10360331
references.citation: J Am Soc Mass Spectrom. 2005 Jan;16(1):71-81
references.pmid: 15653365
references.citation: Anal Chem. 2009 May 1;81(9):3645-53
references.pmid: 19326898
references.citation: Mass Spectrom Rev. 2009 Sep-Oct;28(5):785-815
references.pmid: 19016300
references.citation: Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9528-33
references.pmid: 15210983
references.citation: J Am Chem Soc. 2003 Oct 15;125(41):12404-5
references.pmid: 14531672
references.citation: Anal Chem. 2006 Jul 1;78(13):4702-8
references.pmid: 16808485
references.citation: J Am Soc Mass Spectrom. 2007 May;18(5):882-90
references.pmid: 17349802