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Antimicrobial cyclic peptides for plant disease control.

Lee DW, Kim BS - Plant Pathol. J. (2015)

Bottom Line: These are specific and selective targets providing reliable activity and safety for non-target organisms.Synthetic cyclic peptides produced through combinatorial chemistry offer an alternative approach to develop antimicrobials for agricultural uses.Those synthesized so far have been studied for antibacterial activity, however, the recent advancements in powerful technologies now promise to provide novel antimicrobial cyclic peptides that are yet to be discovered from natural resources.

View Article: PubMed Central - PubMed

Affiliation: Plant Pharmacology Laboratory, Department of Biosystems and Biotechnology, College of Life Science and Biotechnology, Korea University, Seoul 136-713, Korea.

ABSTRACT
Antimicrobial cyclic peptides derived from microbes bind stably with target sites, have a tolerance to hydrolysis by proteases, and a favorable degradability under field conditions, which make them an attractive proposition for use as agricultural fungicides. Antimicrobial cyclic peptides are classified according to the types of bonds within the ring structure; homodetic, heterodetic, and complex cyclic peptides, which in turn reflect diverse physicochemical features. Most antimicrobial cyclic peptides affect the integrity of the cell envelope. This is achieved through direct interaction with the cell membrane or disturbance of the cell wall and membrane component biosynthesis such as chitin, glucan, and sphingolipid. These are specific and selective targets providing reliable activity and safety for non-target organisms. Synthetic cyclic peptides produced through combinatorial chemistry offer an alternative approach to develop antimicrobials for agricultural uses. Those synthesized so far have been studied for antibacterial activity, however, the recent advancements in powerful technologies now promise to provide novel antimicrobial cyclic peptides that are yet to be discovered from natural resources.

No MeSH data available.


Molecular structures of cyclic peptides with unknown antimicrobial mechanisms.
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f3-ppj-31-1: Molecular structures of cyclic peptides with unknown antimicrobial mechanisms.

Mentions: Cepacidines A1 and A2 (Fig. 3) are glycopeptides produced by Pseudomonas cepacia (Lee et al., 1994; Lim et al., 1994). The MICs for cepacidine A range from 0.098 to 0.391 mg/ml against Aspergillus niger, F. oxysporum, and Rhizopus stolonifer. Fungicin M4 is a hydrophilic antifungal peptide produced by Bacillus licheniformis M-4 (Lebbadi et al., 1994). Fungicin M4 is resistant to proteolytic enzymes and lipase, and inhibits the growth of Microsporum canis, Mucor species, Bacillus megaterium, Corynebacterium glutamicum, and Sporothrix schenckii. Peptide antibiotic PKB1 (Fig. 3) is produced by P. polymyxa PKB1 and has antifungal activity against the causative agent of blackleg disease in canola (Leptosphaeria maculans) as well as other economically destructive pathogens including S. sclerotiorum, Marasmius oreades, Pythium pythioides, R. solani, Fusarium avenaceum, and Alternaria brassicae (Kharbanda et al., 2003). P. polymyxa PKB1 can also act as a biocontrol agent against blackleg and other fungal diseases of canola. Success in using P. polymyxa PKB1 as a biocontrol agent was achieved by coating canola seeds with freeze-dried or living cells of the bacterium to protect germinating shoots from L. maculans infection in stubble.


Antimicrobial cyclic peptides for plant disease control.

Lee DW, Kim BS - Plant Pathol. J. (2015)

Molecular structures of cyclic peptides with unknown antimicrobial mechanisms.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4356600&req=5

f3-ppj-31-1: Molecular structures of cyclic peptides with unknown antimicrobial mechanisms.
Mentions: Cepacidines A1 and A2 (Fig. 3) are glycopeptides produced by Pseudomonas cepacia (Lee et al., 1994; Lim et al., 1994). The MICs for cepacidine A range from 0.098 to 0.391 mg/ml against Aspergillus niger, F. oxysporum, and Rhizopus stolonifer. Fungicin M4 is a hydrophilic antifungal peptide produced by Bacillus licheniformis M-4 (Lebbadi et al., 1994). Fungicin M4 is resistant to proteolytic enzymes and lipase, and inhibits the growth of Microsporum canis, Mucor species, Bacillus megaterium, Corynebacterium glutamicum, and Sporothrix schenckii. Peptide antibiotic PKB1 (Fig. 3) is produced by P. polymyxa PKB1 and has antifungal activity against the causative agent of blackleg disease in canola (Leptosphaeria maculans) as well as other economically destructive pathogens including S. sclerotiorum, Marasmius oreades, Pythium pythioides, R. solani, Fusarium avenaceum, and Alternaria brassicae (Kharbanda et al., 2003). P. polymyxa PKB1 can also act as a biocontrol agent against blackleg and other fungal diseases of canola. Success in using P. polymyxa PKB1 as a biocontrol agent was achieved by coating canola seeds with freeze-dried or living cells of the bacterium to protect germinating shoots from L. maculans infection in stubble.

Bottom Line: These are specific and selective targets providing reliable activity and safety for non-target organisms.Synthetic cyclic peptides produced through combinatorial chemistry offer an alternative approach to develop antimicrobials for agricultural uses.Those synthesized so far have been studied for antibacterial activity, however, the recent advancements in powerful technologies now promise to provide novel antimicrobial cyclic peptides that are yet to be discovered from natural resources.

View Article: PubMed Central - PubMed

Affiliation: Plant Pharmacology Laboratory, Department of Biosystems and Biotechnology, College of Life Science and Biotechnology, Korea University, Seoul 136-713, Korea.

ABSTRACT
Antimicrobial cyclic peptides derived from microbes bind stably with target sites, have a tolerance to hydrolysis by proteases, and a favorable degradability under field conditions, which make them an attractive proposition for use as agricultural fungicides. Antimicrobial cyclic peptides are classified according to the types of bonds within the ring structure; homodetic, heterodetic, and complex cyclic peptides, which in turn reflect diverse physicochemical features. Most antimicrobial cyclic peptides affect the integrity of the cell envelope. This is achieved through direct interaction with the cell membrane or disturbance of the cell wall and membrane component biosynthesis such as chitin, glucan, and sphingolipid. These are specific and selective targets providing reliable activity and safety for non-target organisms. Synthetic cyclic peptides produced through combinatorial chemistry offer an alternative approach to develop antimicrobials for agricultural uses. Those synthesized so far have been studied for antibacterial activity, however, the recent advancements in powerful technologies now promise to provide novel antimicrobial cyclic peptides that are yet to be discovered from natural resources.

No MeSH data available.