Title : The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state.

Pub. Date : 2017 Oct

PMID : 28802697






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The MP1-lipid membrane interaction was studied using Langmuir phosphatidylcholine and phosphatidylserine (PS) monolayers as model membrane systems. Phosphatidylserines pitrilysin metallopeptidase 1 Homo sapiens
2 The MP1-lipid membrane interaction was studied using Langmuir phosphatidylcholine and phosphatidylserine (PS) monolayers as model membrane systems. Phosphatidylserines pitrilysin metallopeptidase 1 Homo sapiens
3 PS was chosen since this negatively charged lipid was found predominantly on the outer leaflet of tumor cells, and it enhances MP1 activity for PS-containing membranes to a greater extent than for other negatively charged lipids. Phosphatidylserines pitrilysin metallopeptidase 1 Homo sapiens
4 PS was chosen since this negatively charged lipid was found predominantly on the outer leaflet of tumor cells, and it enhances MP1 activity for PS-containing membranes to a greater extent than for other negatively charged lipids. Phosphatidylserines pitrilysin metallopeptidase 1 Homo sapiens
5 MP1 incorporated into anionic PS monolayers, which show a liquid-expanded (LE) phase or LE-liquid-condensed (LC) phase coexistence, up to lipid-packing densities higher than those of cell membranes. Phosphatidylserines pitrilysin metallopeptidase 1 Homo sapiens