Journal
ANALYTICAL CHEMISTRY
Volume 90, Issue 8, Pages 5139-5146Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.7b05230
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Funding
- NSF CAREER [CHE-1654274]
- Division of Molecular and Cellular Biosciences
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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.
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