• Publications
  • Influence
Interactome Analyses Identify Ties of PrPC and Its Mammalian Paralogs to Oligomannosidic N-Glycans and Endoplasmic Reticulum-Derived Chaperones
TLDR
A simple hypothesis is presented which accounts for the majority of interactions observed in uninfected cells and suggests that PrPC organizes its molecular environment on account of its ability to bind to adhesion molecules harboring immunoglobulin-like domains, which in turn recognize oligomannose-bearing membrane proteins. Expand
Investigating the effects of L- to D-amino acid substitution and deamidation on the activity and membrane interactions of antimicrobial peptide anoplin.
TLDR
The results suggest that amidated forms of peptides are likely to possess higher membrane binding affinity due to the increased charge and membrane lytic activity of all derivatives was found to depend strongly on membrane composition and lipid/peptide ratio. Expand
Imaging the membrane lytic activity of bioactive peptide latarcin 2a.
TLDR
Interactions of these two ltc2a derivatives with supported "raft" lipid bilayer were studied by in situ atomic force microscopy to investigate the potential anticancer activity of the peptides since some breast and prostate cancer cell lines contain higher levels of cholesterol-rich lipid rafts than non-cancer cells. Expand
Interactions of antimicrobial peptide from C-terminus of myotoxin II with phospholipid mono- and bilayers.
  • Amy Won, A. Ianoul
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 1 October 2009
TLDR
Results of the study indicate that electrostatic interactions play a significant role in the initial recognition and binding of pEM-2 to the cell membrane, however, membrane rupturing activity of the peptide depends on interactions other than simple ionic attraction. Expand
Investigating the effect of a single glycine to alanine substitution on interactions of antimicrobial peptide latarcin 2a with a lipid membrane
TLDR
Data indicate that decrease in the flexibility of ltc2a induced by the modification in the hinge region is likely to increase the peptide’s nonspecific interactions with zwitterionic cell membranes and potentially increase its toxicity against eukaryotic cells. Expand
Effect of point mutations on the secondary structure and membrane interaction of antimicrobial peptide anoplin.
Anoplin (GLLKRIKTLL-NH2) is the smallest linear α-helical antimicrobial peptide found naturally to date. Antibacterial and hemolytic properties of anoplin depend strongly on physicochemicalExpand
Imaging interactions of cationic antimicrobial peptides with model lipid monolayers using X-ray spectromicroscopy
TLDR
X-ray spectromicroscopy is shown to be a valuable quantitative tool for label-free imaging of lipid monolayers with antimicrobial peptides at a lateral spatial resolution below 80 nm. Expand
Effect of point mutations on the secondary structure and membrane interaction of antimicrobial peptide anoplin.
TLDR
Overall the data indicate that antimicrobial activity of anoplin increases with charge, whereas membrane lytic activity correlates with peptides helicity and amphipathicity. Expand
Interaction Between Lytic Peptide Latarcin 2A and Supported Lipid Bilayers Studied by in Situ Atomic Force Microscopy
Latarcin 2a (ltc2a, GLFGKLIKKFGRKAISYAVKKARGKH-COOH) is one of the seven short linear antimicrobial and cytolytic peptides extracted from the venom of the Central Asian spider, Lachesana tarabaevi,Expand
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