National Physical Laboratory

Molecular biophysics of membrane-active peptides: from mono molecular interactions to peptide assembly

Further Information

Published: 23 July 2013

Authors: Jascindra Ravi, Baptiste Lamarre, Eleonora Cerasoli, Lloyd Ryan, Paulina Rakowska, Maxim G Ryadnov

Download (PDF 2 MB)


The understanding of protein structure, assembly and function relationships at biomolecular interface is critical in underpinning the mechanisms governing many biological functions and protein misfolding disorders.

In the search for methods to study the interaction of peptides and proteins with biological membranes, linear dichroism (LD) spectroscopy has emerged as a powerful technique. LD relates shear-aligned phospholipid membranes with conformation and binding geometries of membrane-bound proteinsand peptides in solution phase. This presentation will highlight how LD spectral features are used to interpret and differentiate membrane-binding mechanisms of membrane-active peptides.

The information gained is unique in that it can provide a rapid and accurate answer to mechanistic aspects of biological function at the molecular level, which is otherwise accessible only by resource costly high-resolution approaches (e.g. NMR or crystallography). Therefore, this solution-based technique holds particular promise in the development of high-throughput approaches in providing solutions to a variety of healthcare problems including bacterial cross-resistance, viral infectivity and amyloidogenesis.

Last Updated: 4 Oct 2016
Created: 29 Apr 2013


Please note that the information will not be divulged to third parties, or used without your permission