LC-Trapped Ion Mobility Spectrometry-TOF MS Differentiation of 2- and 3-Disulfide-Bonded Isomers of the μ-Conotoxin PIIIA

Autor:	Detlev Suckau, Diana Imhof, Thomas Schmitz, Stuart Pengelley, Eckhard Belau
Rok vydání:	2020
Předmět:	Chemistry Ion-mobility spectrometry Stereochemistry Disulfide bond Mass Spectrometry Analytical Chemistry Isomerism Ion Mobility Spectrometry Amino Acid Sequence Disulfides Time-of-flight mass spectrometry Conotoxins μ conotoxin Chromatography Liquid
Zdroj:	Analytical Chemistry. 92:10920-10924
ISSN:	1520-6882 0003-2700
DOI:	10.1021/acs.analchem.0c02151
Popis:	Disulfide bonds within cysteine-rich peptides are important for their stability and biological function. In this respect, the correct disulfide connectivity plays a decisive role. The differentiation of individual disulfide-bonded isomers by traditional high-performance liquid chromatography (HPLC) and mass spectrometry (MS) is limited due to the similarity in physicochemical properties of the isomers sharing the same amino acid sequence. By using trapped ion mobility spectrometry-mass spectrometry (TIMS-MS), several 2- and 3-disulfide-bonded isomers of the μ-conotoxin PIIIA were investigated for their distinguishability by collision cross section (CCS) values and their characteristic mobilogram traces. The isomers could be differentiated by TIMS-MS and also identified in mixing experiments. Thus, TIMS-MS provides a highly valuable and enriching addition to standard HPLC and MS analysis of conformational isomers of disulfide-rich peptides and proteins.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afc6885c3ca29ac84929a38310c8b4f9 https://doi.org/10.1021/acs.analchem.0c02151 Zobrazit plný text záznamu