Insertion of antimicrobial peptides into phospholipid monolayers at air/liquid interface: effects of unnatural cationic amino acids

DOI

We have designed a series of cationic peptides with different helix repeats that can kill bacteria but remain benign to mammalian host cells. The selectivity to cell types is well correlated to their responses to different model lipid monolayers mimicking the out membranes of different cell types. We propose to use neutron reflection to explore the basic structural features of different interactions between these small peptides and different model lipid monolayers bearing charge and structural characteristics. In particular, this work focus on assessing the impacts of unnatural cationic amino acids in bacterial killing by determining the amount and location of membrane associated peptides bearing these unnatural amino acids.

Identifier
DOI https://doi.org/10.5286/ISIS.E.47833461
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/47833461
Provenance
Creator Dr Zongyi Li; Professor Jiqian Wang; Mr Elias Pambou; Dr Xiubo (Jon) Zhao; Mr Zhiming Lu; Dr Mario Campana; Professor Jian Lu; Miss Silvia Cirillo
Publisher ISIS Neutron and Muon Source
Publication Year 2017
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 2014-03-12T00:00:00Z
Temporal Coverage End 2014-05-21T06:32:51Z