Tailoring the volatility and stability of oligopeptides

Autor(en)

J. Schatti, U. Sezer, S. Pedalino, J. P. Cotter, M. Arndt, M. Mayor, V. Köhler

Abstrakt

Amino acids are essential building blocks of life, and fluorinated derivatives have gained interest in chemistry and medicine. Modern mass spectrometry has enabled the study of oligo- and polypeptides as isolated entities in the gas phase, but predominantly as singly or even multiply charged species. While laser desorption of neutral peptides into adiabatically expanding supersonic noble gas jets is possible, UV–VIS spectroscopy, electric or magnetic deflectometry as well as quantum interferometry would profit from the possibility to prepare thermally slow molecular beams. This has typically been precluded by the fragility of the peptide bond and the fact that a peptide would rather ‘fry’, i.e. denature and fragment than ‘fly’. Here, we explore how tailored perfluoroalkyl functionalization can reduce the intermolecular binding and thus increase the volatility of peptides and compare it to previously explored methylation, acylation and amidation of peptides. We show that this strategy is essential and enables the formation of thermal beams of intact neutral tripeptides, whereas only fragments were observed for an extensively fluoroalkyl-decorated nonapeptide.

Organisation(en)

Quantenoptik, Quantennanophysik und Quanteninformation

Externe Organisation(en)

Universität Basel, Karlsruher Institut für Technologie

Journal

Journal of Mass Spectrometry

Band

52

Seiten

550-556

Anzahl der Seiten

7

ISSN

1076-5174

DOI

https://doi.org/10.1002/jms.3959

Publikationsdatum

08-2017

Peer-reviewed

Ja

ÖFOS 2012

103006 Chemische Physik

Schlagwörter

ASJC Scopus Sachgebiete

Spectroscopy

Link zum Portal

https://ucrisportal.univie.ac.at/de/publications/d4976fa2-321a-41c7-815c-6d4fb43586ab