Interactions of designed helix peptides with 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 different charge and structural characteristics. In particular, this work focus on assessing the different impacts of unnatural cationic amino acids in bacterial killing by gaining insight in the amount and location of insertion of the peptides bearing these unnatural amino acids into different model lipid interfaces.

Identifier
DOI https://doi.org/10.5286/ISIS.E.42588237
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/42588237
Provenance
Creator Dr Mario Campana; Professor Jiqian Wang; Dr Zongyi Li; Miss Shuyi Han; Mr Zhiming Lu; Mr Elias Pambou; Professor Jian Lu; Dr Xiubo (Jon) Zhao; Mr Dharana Jayawardane
Publisher ISIS Neutron and Muon Source
Publication Year 2016
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 Photon- and Neutron Geosciences
Temporal Coverage Begin 2013-09-28T23:00:00Z
Temporal Coverage End 2013-09-30T23:00:00Z