• The Plant Pathology Journal
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• 제31권1호
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• pp.1-11
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• 2015

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.

• Journal of Dairy Science and Biotechnology
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• 제30권1호
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• pp.37-44
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• 2012

Milk-derived bioactive peptides have been found to exhibit various physiological activities such as angiotensin-converting enzyme (ACE) inhibitory, antibacterial, and antioxidative effects. Bioactive peptides can be used in the formulation of functional foods, nutraceuticals, and natural drugs because of their beneficial effects. However, the degree of variability in the composition, functionality, and sensory properties of such peptides has greatly limited their use in the food industry. In this review, we discuss the main peptides obtained from milk proteins and summarize findings from previous studies on the production and biological activities of these peptides. In addition, we compare the methods used to separate and identify the structure of the bioactive peptides and highlight current investigations into engineering and implementation of technologies that would allow more efficient isolation of bioactive peptides for functional food production. To improve human health, further molecular biology studies will also be required to elucidate the complex network of interactions between food microorganisms and the digestive system.

• BMB Reports
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• 제29권6호
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• pp.545-548
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• 1996

CA(1-8)ME(1-12), the CA-ME hybrid peptide of the amino terminal segments of cecropin A (CA) and melittin (ME), has been reported to have a broad spectrum and improved potency without a hemolytic property. In order to obtain new synthetic peptides with powerful antibacterial activity without hemolytic activity, several hybrid peptides were designed from the sequences of CA, ME, magainin 2, bombinin and lactoferricin. All hybrid peptides were constructed to form an amphipathically basic-flexible-hydrophobic structure and synthesized by the solid phase method. Their hemolytic activities against human red blood cells and antibacterial activities against both Gram-positive and Gram-negative bacteria were detennined. CA(1-8)MA(1-12), CA(1-8)BO(1-12), MA(10-17)ME(1-12) and LF(20-29)ME(1-12) showed comparable activities with broad spectra against both Gram-positive and Gram-negative bacteria relative to CA(1-8)ME(1-12) but without hemolytic properties. These hybrid peptides, therefore, could be useful as model peptides to design a novel peptide with improved antibacterial activity and study on structure-activity relationships of antimicrobial peptides.

• IMMUNE NETWORK
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• 제11권5호
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• pp.245-252
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• 2011

Antimicrobial peptides/proteins are ancient and naturally-occurring antibiotics in innate immune responses in a variety of organisms. Additionally, these peptides have been recognized as important signaling molecules in regulation of both innate and adaptive immunity. During mycobacterial infection, antimicrobial peptides including cathelicidin, defensin, and hepcidin have antimicrobial activities against mycobacteria, making them promising candidates for future drug development. Additionally, antimicrobial peptides act as immunomodulators in infectious and inflammatory conditions. Multiple crucial functions of cathelicidins in antimycobacterial immune defense have been characterized not only in terms of direct killing of mycobacteria but also as innate immune regulators, i.e., in secretion of cytokines and chemokines, and mediating autophagy activation. Defensin families are also important during mycobacterial infection and contribute to antimycobacterial defense and inhibition of mycobacterial growth both in vitro and in vivo. Hepcidin, although its role in mycobacterial infection has not yet been characterized, exerts antimycobacterial effects in activated macrophages. The present review focuses on recent efforts to elucidate the roles of host defense peptides in innate immunity to mycobacteria.

• 대한치과의사협회지
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• 제41권2호통권405호
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• pp.116-123
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• 2003

Antimicrobial Peptides are natural antibiotics evolved by many plants, invertebrate, and vertebrate to defend against the microbial infection. Antimicrobial peptides show a broad-spectrum antimicrobial activity with little opportunity for the development of resistance since they target microbial membranes that distinguish microbes from enkaryotic cells. The oral cavity is constantly exposed to microbial challenges and antimicrobial peptides play an important role in managing the oral health. With the increase of resistant micro-organisms to conventional antibiotics, antimicrobial peptides are attracting interests as novel antibiotics. In this review, the characteristics of antimicrobial of antimicrobial peptides including the classification, mechanism of action, resistance, and expression in the oral cavity have been discussed in the prospects of application to oral disease.

• Animal cells and systems
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• 제2권3호
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• pp.361-365
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• 1998

Antimicrobial peptides are widely distributed in nature and appear to play important roles in the host defense of plants and animals. In this study, we isolated and characterized three antimicrobial peptides from skin secretions of the oriental fire-bellied toad, Bombina orientalis. These purified peptides were referred to as P1, P2, and P3 in order of their elution. P1, P2, and P3 have molecular weights of 2569, 2566, and 2370 Da by MALDI-TOF mass spectrometer, respectively. They are heat-stable, amphipathic peptides of 24-27 amino acids without cysteine residues. All three peptides are active against representative gram negative and gram positive bacterial species, and in particular, P1 appears to have distinctive antifungal activity. However, no significant hemolytic activity was found for these peptides.

• KSBB Journal
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• 제27권1호
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• pp.9-15
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• 2012

Antimicrobial peptides are widely used in various organisms as a defense system against infection. The peptides are lethal towards bacteria and fungi, however have minimal toxicity in mammalian and plant cells. In this aspect, it is considered that antimicrobial peptides are new alternative materials for defensing against microbial infection. Here, we describe overall characteristics of antimicrobial peptides based on the mechanism of action, classification of the peptides, report detection/screening methods and chemical/biological production. It is expected that understanding of innate immune system based on antimicrobial peptides tends to develop novel natural antimicrobial agents, which might be applied for defensing pathogenic microorganisms resistant to conventional antibiotics.

• Fisheries and Aquatic Sciences
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• 제22권5호
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• pp.10.1-10.14
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• 2019

Fish skin waste accounts for part of the solid waste generated from seafood processing. Utilization of fish skin by bioconversion into high-grade products would potentially reduce pollution and economic cost associated with treating fish processing waste. Fish skin is an abundant supply of gelatin and collagen which can be hydrolyzed to produce bioactive peptides of 2-20 amino acid sequences. Bioactivity of peptides purified from fish skin includes a range of activities such as antihypertensive, anti-oxidative, antimicrobial, neuroprotection, antihyperglycemic, and anti-aging. Fish skin acts as a physical barrier and chemical barrier through antimicrobial peptide innate immune action and other functional peptides. Small peptides have been demonstrated to possess biological activities which are based on their amino acid composition and sequence. Fish skin-derived peptides contain a high content of hydrophobic amino acids which contribute to the antioxidant and angiotensin-converting enzyme inhibitory activity. The peptide-specific composition and sequence discussed in this review can be potentially utilized in the development of pharmaceutical and nutraceutical products.

• 분석과학
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• 제8권4호
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• pp.849-854
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• 1995

A series of biologically active phosphopeptides were synthesized and their behavior in tandem mass spectrometry have been investigated. The structure identifications of other unusual peptides such as sulphated, glycosylated, lipoidal, and backbone modified peptides have been carried out. For all tested peptides, the structural modification could be determined directly by measurement of the absolute molecular weight in combination with collision-induced-dissociation in tandem mass spectrometry.

• BMB Reports
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• 제28권6호
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• pp.546-551
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• 1995

The conformation studies of myelin P2 protein and two of its major peptides were carried out using circular dichroism and fluorescence spectroscopy in water and in lipid environments. Significant conformational changes occur when the protein or peptides were bound to gangliosides. Similar effects were also found in trifluoroethanol solutions. The conformational features of P2 protein and its major peptides were discussed in relation to the environmental changes and the disease-inducing effects.