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Anti-biofilm and sporicidal activity of peptides based on wheat puroindoline and barley hordoindoline proteins.

Authors :
Shagaghi N
Alfred RL
Clayton AH
Palombo EA
Bhave M
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.)

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