Elucidating molecular mechanism of membrane disruption by designed α-helix peptides with antitumor and antibacterial properties

DOI

We have previously shown that peptides such as G(IIKK)4I-NH2 (G4) can kill bacteria and inhibit cancer cell growth whilst remaining benign to mammalian host cells. We have also demonstrated using Langmuir trough measurements that these peptides can selectively respond to different membrane types and that charge interaction is a crucial factor . Here we propose to use neutron reflection to study how these peptide interact with lipid monolayers under different surface pressures. As peptide binding follows a dynamic process over a period of 30-60 min during which the surface pressure rises steadily, we will plan measurements under different contrasts with a carefully select set of pressure and time windows.

Identifier
DOI https://doi.org/10.5286/ISIS.E.81735398
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/81735398
Provenance
Creator Dr Zongyi Li; Dr Arwel Hughes; Professor Jian Lu; Dr John Webster; Miss Daniela Ciumac; Dr Mario Campana; Mr Ruiheng Li
Publisher ISIS Neutron and Muon Source
Publication Year 2019
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Natural Sciences; Physics
Temporal Coverage Begin 2016-07-24T08:00:00Z
Temporal Coverage End 2016-07-26T08:00:00Z