Design of self‐processing antimicrobial peptides for plant protection
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 prot...
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Veröffentlicht in: | Letters in applied microbiology 2000-08, Vol.31 (2), p.163-168 |
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Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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. |
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ISSN: | 0266-8254 1472-765X 1365-2673 |
DOI: | 10.1046/j.1365-2672.2000.00782.x |