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Design of self‐processing antimicrobial peptides for plant protection
Author(s) -
Powell W.A.,
Catranis C.M.,
Maynard C.A.
Publication year - 2000
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1046/j.1365-2672.2000.00782.x
Subject(s) - antimicrobial , antimicrobial peptides , peptide , protease , tobacco etch virus , amino acid , biology , biochemistry , plant protein , microbiology and biotechnology , pathogen , plant virus , chemistry , virus , enzyme , virology , food science , potyvirus
Small antimicrobial peptides are excellent candidates for inclusion in self‐processing proteins that could be used to confer pathogen resistance in transgenic plants. Antimicrobial peptides as small as 22 amino acids in length have been designed to incorporate the residual amino acids left from protein processing by the tobacco etch virus'(TEVs') NIa protease. Also, by minimizing the length of these peptides and the number of highly hydrophobic residues, haemolytic activity was reduced without affecting the peptide's antimicrobial activity.