Lipid Domains in the Membrane:  Thermotropic Properties of Sphingomyelin Vesicles Containing GM1 Ganglioside and Cholesterol†

Biochemistry ◽  
1997 ◽  
Vol 36 (30) ◽  
pp. 9232-9236 ◽  
Author(s):  
Anita Ferraretto ◽  
Marina Pitto ◽  
Paola Palestini ◽  
Massimo Masserini
Keyword(s):  
Gm1 Ganglioside ◽  
Lipid Domains ◽  
Thermotropic Properties

scholarly journals Generalized CNS Disease and Massive GM1-Ganglioside Accumulation in Mice Defective in Lysosomal Acid  -galactosidase

1997 ◽  
Vol 6 (2) ◽  
pp. 205-211 ◽  
Author(s):  
C. N. Hahn ◽  
M. del Pilar Martin ◽  
M. Schroder ◽  
M. T. Vanier ◽  
K. Suzuki ◽  
...  
Keyword(s):  
Gm1 Ganglioside ◽  
Lysosomal Acid ◽  
Cns Disease

scholarly journals Insights into the Action Mechanism of the Antimicrobial Peptide Lasioglossin III

2021 ◽  
Vol 22 (6) ◽  
pp. 2857
Author(s):  
Filomena Battista ◽  
Rosario Oliva ◽  
Pompea Del Vecchio ◽  
Roland Winter ◽  
Luigi Petraccone
Keyword(s):  
Antimicrobial Peptide ◽  
Gram Negative Bacteria ◽  
Lipid Domains ◽  
Action Mechanism ◽  
Cationic Antimicrobial Peptide ◽  
Intracellular Targeting ◽  
Gel Retardation Assay ◽  
Charged Membrane ◽  
Intracellular Target ◽  
Anionic Lipids

Lasioglossin III (LL-III) is a cationic antimicrobial peptide derived from the venom of the eusocial bee Lasioglossum laticeps. LL-III is extremely toxic to both Gram-positive and Gram-negative bacteria, and it exhibits antifungal as well as antitumor activity. Moreover, it shows low hemolytic activity, and it has almost no toxic effects on eukaryotic cells. However, the molecular basis of the LL-III mechanism of action is still unclear. In this study, we characterized by means of calorimetric (DSC) and spectroscopic (CD, fluorescence) techniques its interaction with liposomes composed of a mixture of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and 1-palmitoyl-2-oleoyl-sn-glycero-3-rac-phosphoglycerol (POPG) lipids as a model of the negatively charged membrane of pathogens. For comparison, the interaction of LL-III with the uncharged POPC liposomes was also studied. Our data showed that LL-III preferentially interacted with anionic lipids in the POPC/POPG liposomes and induces the formation of lipid domains. Furthermore, the leakage experiments showed that the peptide could permeabilize the membrane. Interestingly, our DSC results showed that the peptide-membrane interaction occurs in a non-disruptive manner, indicating an intracellular targeting mode of action for this peptide. Consistent with this hypothesis, our gel-retardation assay experiments showed that LL-III could interact with plasmid DNA, suggesting a possible intracellular target.

scholarly journals Ordered Lipid Domains Assemble via Concerted Recruitment of Constituents from Both Membrane Leaflets

2019 ◽  
Vol 116 (3) ◽  
pp. 328a
Author(s):  
Ali Saitov ◽  
Sergey A. Akimov ◽  
Timur R. Galimzyanov ◽  
Toma N. Glasnov ◽  
Peter Pohl
Keyword(s):  
Lipid Domains

scholarly journals Novel GM1 ganglioside-like peptide mimics prevent the association of cholera toxin to human intestinal epithelial in vitro

Glycobiology ◽  
2016 ◽  
Vol 26 (5) ◽  
pp. 540-540 ◽  
Author(s):  
Robert K Yu ◽  
Seigo Usuki ◽  
Yutaka Itokazu ◽  
Han-Chung Wu
Keyword(s):  
Cholera Toxin ◽  
Gm1 Ganglioside ◽  
Intestinal Epithelial ◽  
Peptide Mimics

F6, anti-GM1 ganglioside

Hybridoma ◽  
1995 ◽  
Vol 14 (1) ◽  
pp. 97-97
Keyword(s):  
Gm1 Ganglioside

scholarly journals The GM1 Ganglioside Forms GM1-Rich Gel Phase Microdomains within Lipid Rafts

Coatings ◽  
2014 ◽  
Vol 4 (3) ◽  
pp. 450-464 ◽  
Author(s):  
Lucia Becucci ◽  
Francesco Vizza ◽  
Yolanda Duarte ◽  
Rolando Guidelli
Keyword(s):  
Lipid Rafts ◽  
Gm1 Ganglioside ◽  
Gel Phase
Sign in / Sign up

Export Citation Format

Share Document