Study of the interfacial self-assembly of peptide/polymer membranes by neutron reflectivity methods

DOI

The interfacial self-assembly between large (polymer) and small (peptide) molecules of opposite charge results in the formation of highly organized membranes. Furhter manipulation of the peptide sequence leads to membranes with distinct surface morphologies, from well-defined micro-grooves to micro-sized aggregates.This proposal aims to investigate how peptide sequence controls the behavior and organization of peptide amphiphiles at the air-water interface and understand their interactions with aqueous polymer solutions.The ability of modulating the surface topography of self-assembled membranes, by introducing subtle changes in the peptide sequence, offers a simple way to develop patterned thin soft membranes with great potential for biomedical applications.

Identifier
DOI https://doi.org/10.5286/ISIS.E.67771157
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/67771157
Provenance
Creator Dr Maxmilian Skoda; Dr Helena Azevedo; Dr Jayati Banerjee; Dr Rebecca Welbourn
Publisher ISIS Neutron and Muon Source
Publication Year 2018
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 Biology; Biomaterials; Engineering Sciences; Life Sciences; Materials Science; Materials Science and Engineering
Temporal Coverage Begin 2015-11-16T09:00:00Z
Temporal Coverage End 2015-11-19T09:00:00Z