Back to Search
Start Over
Identification of Lasso Peptide Topologies Using Native Nanoelectrospray Ionization-Trapped Ion Mobility Spectrometry-Mass Spectrometry.
- Source :
-
Analytical Chemistry . 4/17/2018, Vol. 90 Issue 8, p5139-5146. 8p. - Publication Year :
- 2018
-
Abstract
- Lasso peptides are a fascinating class of bioactive ribosomal natural products characterized by a mechanically interlocked topology. In contrast to their branched-cyclic forms, lasso peptides have higher stability and have become a scaffold for drug development. However, the identification and separation of lasso peptides from their unthreaded topoisomers (branched-cyclic peptides) is analytically challenging since the higher stability is based solely on differences in their tertiary structures. In the present work, a fast and effective workflow is proposed for the separation and identification of lasso from branched cyclic peptides based on differences in their mobility space under native nanoelectrospray ionization-trapped ion mobility spectrometry-mass spectrometry (nESI-TIMS-MS). The high mobility resolving power (R) of TIMS resulted in the separation of lasso and branched-cyclic topoisomers (R up to 250, 150 needed on average). The advantages of alkali metalation reagents (e.g., Na, K, and Cs salts) as a way to increase the analytical power of TIMS is demonstrated for topoisomers with similar mobilities as protonated species, efficiently turning the metal ion adduction into additional separation dimensions. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00032700
- Volume :
- 90
- Issue :
- 8
- Database :
- Academic Search Index
- Journal :
- Analytical Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 129223977
- Full Text :
- https://doi.org/10.1021/acs.analchem.7b05230