RT Journal Article
T1 Biophysical approaches to study actinoporin-lipid interactions
A1 Palacios Ortega, Juan
A1 Rivera de Torre, Esperanza
A1 Gavilanes Franco, José Gregorio
A1 Slotte, J. Peter
A1 Martínez Del Pozo, Álvaro
A1 García Linares, Sara
AB Protein-lipid interactions are crucial events from a biochemical point of view, like the interaction of proteins with the cell plasma membrane, and their study is of great importance. Actinoporins are a very powerful tool to study this kind of interactions, since they are soluble proteins in an aqueous environment, capable of inserting into membranes when they have the adequate composition. In fact, actinoporins have been used to study protein-lipid interactions for many years now. Sometimes it is not possible to use real biological membranes in the experiments, so model membranes need to be used. This article aims to give a thorough description of many of the techniques used to study actinoporin-lipid interactions, using both biological and model membranes: Hemolysis, release of vesicles content, surface plasmon resonance, isothermal titration calorimetry, fluorescence-based measurements, etc. Some of these techniques measure the actinoporins activity and some measure their binding properties. The combination of all the techniques described can offer valuable information about the thermodynamics and the kinetics of the actinoporin-lipid interaction.
PB Elsevier
YR 2021
FD 2021-08-01
LK https://hdl.handle.net/20.500.14352/110961
UL https://hdl.handle.net/20.500.14352/110961
LA eng
NO Juan Palacios-Ortega, Esperanza Rivera-de-Torre, José G. Gavilanes, J. Peter Slotte, Álvaro Martínez-del-Pozo, Sara García-Linares, Chapter Eleven - Biophysical approaches to study actinoporin-lipid interactions, Editor(s): Alejandro P. Heuck, Methods in Enzymology, Academic Press, Volume 649, 2021, Pages 307-339, ISSN 0076-6879, ISBN 9780128238585, https://doi.org/10.1016/bs.mie.2020.12.017. (https://www.sciencedirect.com/science/article/pii/S0076687920303839)
NO Banco Santander
DS Docta Complutense
RD 8 abr 2025