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Pore‐forming peptide of Entamoeba histolytica significance of positively charged amino acid residues for its mode of action
Author(s) -
Andrä Jörg,
Leippe Matthias
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01103-6
Subject(s) - histidine , lysine , peptide , entamoeba histolytica , residue (chemistry) , chemistry , biochemistry , cytolysis , vesicle , chemical modification , cationic polymerization , mode of action , amino acid , acetylation , membrane , stereochemistry , biology , organic chemistry , in vitro , cytotoxicity , microbiology and biotechnology , gene
Amoebapore is a 77‐residue pore‐forming peptide from Entamoeba histolytica with antibacterial and cytolytic properties. It contains eight lysine residues and one histidine residue. Chemical modifications of amoebapore with various reagents affecting either both types of cationic residues or lysine and histidine residues separately resulted in virtually complete loss of pore‐forming activity. The activity was restored by reversal of modifications. Whereas amoebapore was no longer capable of binding to phospholipid vesicles when its lysine residues were modified, the modification of the single histidine primarily affected oligomerization of the peptide upon membrane association.