Formation of Neutral Peptide Aggregates as Studied by Mass-Selective IR Action Spectroscopy

Sjors Bakels, Sebastiaan B.A. Porskamp, Anouk M. Rijs*

*Corresponding author for this work

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

The spontaneous aggregation of proteins and peptides is widely studied owing to its relation to neurodegenerative diseases. To understand the underlying principles of peptide aggregation, elucidation of structure and structural changes upon their formation is key. This level of detail can be obtained by studying the peptide self-assembly in the gas phase. Structural characterization of aggregates is mainly done on charged species, as adding charges is an intrinsic part of the technique to bring molecules into the gas phase. Studying neutral peptide aggregates will complement the existing picture. These studies are restricted to dimers due to experimental limitations. Herein, we present advances in laser desorption molecular beam spectroscopy to form neutral peptide aggregates consisting of up to 14 monomeric peptides in the gas phase. The combination of this technique with IR–UV spectroscopy allowed us to select each aggregate by size and subsequently characterize its structure.

Original languageEnglish
Pages (from-to)10537-10541
Number of pages5
JournalAngewandte Chemie - International Edition
Volume58
Issue number31
DOIs
Publication statusPublished - 29 Jul 2019
Externally publishedYes

Keywords

  • aggregation
  • IR spectroscopy
  • laser desorption
  • peptides
  • self-assembly

Fingerprint

Dive into the research topics of 'Formation of Neutral Peptide Aggregates as Studied by Mass-Selective IR Action Spectroscopy'. Together they form a unique fingerprint.

Cite this