English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Zwitterionic character and lipid composition determine the behaviour of GPI fragments in monolayers

MPS-Authors
/persons/resource/persons213957

Malik,  Ankita
Daniel Varón Silva, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons121849

Seeberger,  Peter H.
Peter H. Seeberger - Vaccine Development, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons121172

Brezesinski,  Gerald
Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons127124

Varón Silva,  Daniel
Daniel Varón Silva, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

Article.pdf
(Publisher version), 5MB

Supplementary Material (public)
There is no public supplementary material available
Citation

Malik, A., Seeberger, P. H., Brezesinski, G., & Varón Silva, D. (2021). Zwitterionic character and lipid composition determine the behaviour of GPI fragments in monolayers. ChemPhysChem, 22(8), 757-763. doi:10.1002/cphc.202100002.


Cite as: https://hdl.handle.net/21.11116/0000-0007-F751-7
Abstract
Glycosylphosphatidylinositols (GPIs) are complex glycolipids found in free form or anchoring proteins to the outer leaflet of the cell membrane in eukaryotes. GPIs have been associated with the formation of lipid rafts and protein sorting on membranes. The presence of a conserved glycan core of cell-specific modifications together with lipid remodeling during biosynthesis suggest that the properties of the glycolipids are being fine tuned. We synthesized a series of GPI fragments and evaluated the interactions and arrangement of these glycolipids in monolayers as a 2-D membrane model. GIXD and IRRAS analyses showed the need of N-acetylglucosamine deacetylation for the formation of hydrogen bonds to obtain highly-structured domains in the monolayers and an effect of the unsaturated lipids in formation and localization of the glycolipids within or between membrane microdomains. These results contribute to understand the role of these glycolipids and their modifications in the organization of membranes.