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Anti-biofilm and sporicidal activity of peptides based on wheat puroindoline and barley hordoindoline proteins.
- Source :
-
Journal of peptide science : an official publication of the European Peptide Society [J Pept Sci] 2016 Jul; Vol. 22 (7), pp. 492-500. Date of Electronic Publication: 2016 May 30. - Publication Year :
- 2016
-
Abstract
- The broad-spectrum activity of antimicrobial peptides (AMPs) and low probability of development of host resistance make them excellent candidates as novel bio-control agents. A number of AMPs are found to be cationic, and a small proportion of these are tryptophan-rich. The puroindolines (PIN) are small, basic proteins found in wheat grains with proposed roles in biotic defence of seeds and seedlings. Synthetic peptides based on their unique tryptophan-rich domain (TRD) display antimicrobial properties. Bacterial endospores and biofilms are highly resistant cells, with significant implications in both medical and food industries. In this study, the cationic PIN TRD-based peptides PuroA (FPVTWRWWKWWKG-NH2 ) and Pina-M (FSVTWRWWKWWKG-NH2 ) and the related barley hordoindoline (HIN) based Hina (FPVTWRWWTWWKG-NH2 ) were tested for effects on planktonic cells and biofilms of the common human pathogens including Pseudomonas aeruginosa, Listeria monocytogenes and the non-pathogenic Listeria innocua. All peptides showed significant bactericidal activity. Further, PuroA and Pina-M at 2 × MIC prevented initial biomass attachment by 85-90% and inhibited >90% of 6-h preformed biofilms of all three organisms. However Hina, with a substitution of Lys-9 with uncharged Thr, particularly inhibited Listeria biofilms. The PIN based peptides were also tested against vegetative cells and endospores of Bacillus subtilis. The results provided evidence that these tryptophan-rich peptides could kill B. subtilis even in sporulated state, reducing the number of viable spores by 4 log units. The treated spores appeared withered under scanning electron microscopy. The results establish the potential of these tryptophan-rich peptides in controlling persistent pathogens of relevance to food industries and human health. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.<br /> (Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.)
- Subjects :
- Amino Acid Sequence
Anti-Bacterial Agents chemistry
Anti-Bacterial Agents isolation & purification
Antimicrobial Cationic Peptides chemistry
Antimicrobial Cationic Peptides isolation & purification
Bacillus subtilis drug effects
Bacillus subtilis growth & development
Bacillus subtilis ultrastructure
Biofilms growth & development
Hordeum chemistry
Hordeum immunology
Listeria drug effects
Listeria growth & development
Listeria monocytogenes drug effects
Listeria monocytogenes growth & development
Microbial Sensitivity Tests
Plankton drug effects
Plankton growth & development
Plant Proteins chemistry
Plant Proteins isolation & purification
Pseudomonas aeruginosa drug effects
Pseudomonas aeruginosa growth & development
Spores, Bacterial growth & development
Spores, Bacterial ultrastructure
Triticum chemistry
Triticum immunology
Tryptophan chemistry
Anti-Bacterial Agents pharmacology
Antimicrobial Cationic Peptides pharmacology
Biofilms drug effects
Plant Proteins pharmacology
Spores, Bacterial drug effects
Subjects
Details
- Language :
- English
- ISSN :
- 1099-1387
- Volume :
- 22
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Journal of peptide science : an official publication of the European Peptide Society
- Publication Type :
- Academic Journal
- Accession number :
- 27238815
- Full Text :
- https://doi.org/10.1002/psc.2895