ISIS Neutron and Muon Source Data Journal

Folding and unfolding of model antimicrobial peptides in aqueous solution

Abstract: Antimicrobial peptides (AMP) are naturally occurring biomolecules which act as a defense mechanisms against disease in a number of different animals, including humans. These peptides often fold into helices which can penetrate into a wide range of microbial membranes and are of recent interest due to their potential as treatment for infectious diseases. AMP helices have a unique as secondary structure: the peptide fold in such a way that one surface of the helix is hydrophobic whilst the other is largely hydrophilic, in principle this arrangement 'matches' the amphiphilic environment presented by biological membranes so that these AMP can easily penetrate across this barrier. Here we propose to investigate the structure of model AMPs in aqueous solutions in order to understand the role of solvation for AMP behaviour in solution.

Principal Investigator: Dr Sylvia McLain
Experimenter: Dr Ric Gillams
Experimenter: Ms Nicola Steinke

DOI: 10.5286/ISIS.E.RB1510066

ISIS Experiment Number: RB1510066

Publisher: STFC ISIS Neutron and Muon Source

Data format: RAW/Nexus
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Data Citation

The recommended format for citing this dataset in a research publication is as:
[author], [date], [title], [publisher], [doi]

For Example:
Dr Sylvia McLain et al; (2015): Folding and unfolding of model antimicrobial peptides in aqueous solution, STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1510066

Data is released under the CC-BY-4.0 license.