ArticleThe journal of physical chemistry letters2016
Submillisecond Dynamics of Mastoparan X Insertion into Lipid Membranes.
Article in The journal of physical chemistry letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 10 citations in OpenAlex.
- A photoswitchable helical peptide with light-controllable interface/transmembrane topology in lipidic membranes.iScience · 2021Article
- Binding, folding and insertion of a β-hairpin peptide at a lipid bilayer surface: Influence of electrostatics and lipid tail packing.Biochimica et biophysica acta. Biomembranes · 2018Article
- Time-resolved measurements of an ion channel conformational change driven by a membrane phase transition.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The mechanism of protein insertion into a lipid bilayer is poorly understood because the kinetics of this process is difficult to measure. We developed a new approach to study insertion of the antimicrobial peptide Mastoparan X into zwitterionic lipid vesicles, using a laser-induced temperature-jump to initiate insertion on the microsecond time scale and infrared and fluorescence spectroscopies to follow the kinetics. Infrared probes the desolvation of the peptide backbone and yields biphasic kinetics with relaxation lifetimes of 12 and 117 μs, whereas fluorescence probes the intrinsic tryptophan residue located near the N-terminus and yields a single exponential phase with a lifetime of 440 μs. Arrhenius analysis of the temperature-dependent rates yields an activation energy for insertion of 96 kJ/mol. These results demonstrate the complexity of the insertion process and provide mechanistic insight into the interplay between peptides and the lipid bilayer required for peptide transport across cellular membranes.
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