Browsing Chemistry by Subject "Oligomerization"
Now showing items 1-7 of 7
-
Characterization of daptomycin oligomerization with perylene excimer fluorescence: Stoichiometric binding of phosphatidylglycerol triggers oligomer formation
(Elsevier, 2012-03)Daptomycin is a lipopeptide antibiotic that binds to and depolarizes bacterial cell membranes. Its antibacterial activity requires calcium and correlates with the content of phosphatidylglycerol in the target membrane. ... -
Investigations on the Oligomerization of Pyolysin, a Cholesterol-Dependent Cytolysin
(University of Waterloo, 2011-01-25)The bacterial toxin pyolysin (PLO) is a member of the family of Cholesterol-Dependent Cytolysins, which form large, oligomeric pores in cholesterol-containing membranes. The general CDC structure has an elongated shape and ... -
Mode of Action of Daptomycin, a Lipopeptide Antibiotic
(University of Waterloo, 2013-01-28)Daptomycin is a lipopeptide antibiotic that contains 13 amino acids and an N-terminally attached fatty acyl residue. The antibiotic kills Gram-positive bacteria by membrane depolarization. It has long been assumed that ... -
Mutual inhibition through hybrid oligomer formation of daptomycin and the semisynthetic lipopeptide antibiotic CB-182,462
(Elsevier, 2013-02)Daptomycin is a clinically important lipopeptide antibiotic that kills Gram-positive bacteria through membrane depolarization. Its activity requires calcium and the presence of phosphatidylglycerol in the target membrane. ... -
Oligomerization and hemolytic properties of the C-terminal domain of pyolysin, a cholesterol-dependent cytolysin
(NRC Research Press, 2013-04)Pyolysin (PLO) belongs to the homologous family of the cholesterol-dependent cytolysins (CDCs), which bind to cell membranes containing cholesterol to form oligomeric pores of large size. The CDC monomer structure consists ... -
Partial oligomerization of pyolysin induced by a disulfide-tethered mutant
(NRC Research Press, 2012-12)The bacterial toxin pyolysin (PLO) belongs to the family of cholesterol-dependent cytolysins (CDCs), which form large, ring-shaped oligomeric pores in cholesterol-containing membranes. Monomeric CDC molecules have a structure ... -
Streptococcus agalactiae CAMP factor: Functional Roles of N- and C-terminal Domains & Target Membrane Effect on Toxin Activity
(University of Waterloo, 2018-05-22)CAMP factor is a well-known pore-forming toxin secreted by Streptococcus agalactiae that forms discrete pores on susceptible membranes whether natural or artificial. This work reports haemolysis and liposome permeabilization ...