Zwitterionic Character and Lipid Composition Determine the Behaviour of Glycosylphosphatidylinositol Fragments in Monolayers. Issue 8 (15th March 2021)
- Record Type:
- Journal Article
- Title:
- Zwitterionic Character and Lipid Composition Determine the Behaviour of Glycosylphosphatidylinositol Fragments in Monolayers. Issue 8 (15th March 2021)
- Main Title:
- Zwitterionic Character and Lipid Composition Determine the Behaviour of Glycosylphosphatidylinositol Fragments in Monolayers
- Authors:
- Malik, Ankita
Seeberger, Peter H.
Brezesinski, Gerald
Varón Silva, Daniel - Abstract:
- 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 with cell‐specific modifications together with lipid remodelling 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. Abstract : Role of glycosylphosphatidylinositols : The glycan and lipid of glycosylphosphatidylinositols (GPIs) contribute to the biophysical properties and interactions of these glycolipids. Using synthetic molecules, we show the role of N ‐acetylglucosamine deacetylation and lipid remodelling in the formation of domains in monolayers as a 2‐D membrane model. These results contribute to disclose the function of GPIs and their modifications in the activity of GPIAbstract: 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 with cell‐specific modifications together with lipid remodelling 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. Abstract : Role of glycosylphosphatidylinositols : The glycan and lipid of glycosylphosphatidylinositols (GPIs) contribute to the biophysical properties and interactions of these glycolipids. Using synthetic molecules, we show the role of N ‐acetylglucosamine deacetylation and lipid remodelling in the formation of domains in monolayers as a 2‐D membrane model. These results contribute to disclose the function of GPIs and their modifications in the activity of GPI glycolipids on the cell membrane. … (more)
- Is Part Of:
- Chemphyschem. Volume 22:Issue 8(2021)
- Journal:
- Chemphyschem
- Issue:
- Volume 22:Issue 8(2021)
- Issue Display:
- Volume 22, Issue 8 (2021)
- Year:
- 2021
- Volume:
- 22
- Issue:
- 8
- Issue Sort Value:
- 2021-0022-0008-0000
- Page Start:
- 757
- Page End:
- 763
- Publication Date:
- 2021-03-15
- Subjects:
- glycosylphosphatidylinositol -- monolayers -- glycolipids -- GPI modifications -- lipids
Chemistry, Physical and theoretical -- Periodicals
541.05 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1439-7641 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/cphc.202100002 ↗
- Languages:
- English
- ISSNs:
- 1439-4235
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3172.310500
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 16576.xml