Gramicidin S and its use in the Treatment of Infected Wounds

Gause, G. F.; Brazhnikova, M. G.

doi:10.1038/154703a0

Cited by 266 publications

(193 citation statements)

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“…Hotchkiss and Dubos (1940) isolated an antimicrobial substance from Bacillus brevis and named as gramicidin, which showed in vitro and in vivo activity against many Gram-positive bacteria. Later, it was reported that Gramicidin is effective against infected wounds of guinea-pig and since then it is being used as a therapeutic agent (Gause and Brazhnikova 1944). In 1941, antimicrobial peptide Tyrocidine was reported with activity against both Gram-positive and Gram-negative bacteria (Zaffiri et al 2012).…”

Section: History Of Antimicrobial Peptidementioning

confidence: 99%

Antimicrobial peptides as natural bio-preservative to enhance the shelf-life of food

et al. 2016

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Antimicrobial peptides (AMPs) are diverse group of natural proteins present in animals, plants, insects and bacteria. These peptides are responsible for defense of host from pathogenic organisms. Chemical, enzymatic and recombinant techniques are used for the synthesis of antimicrobial peptides. These peptides have been found to be an alternative to the chemical preservatives. Currently, nisin is the only antimicrobial peptide, which is widely utilized in the preservation of food. Antimicrobial peptides can be used alone or in combination with other antimicrobial, essential oils and polymeric nanoparticles to enhance the shelf-life of food. This review presents an overview on different types of antimicrobial peptides, purification techniques, mode of action and application in food preservation.

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Section: History Of Antimicrobial Peptidementioning

confidence: 99%

Antimicrobial peptides as natural bio-preservative to enhance the shelf-life of food

et al. 2016

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“…The cyclic decapeptide antibiotic gramicidin S [cyclo-(Val-Orn-Leu-D-Phe-Pro)2-] was isolated by Gause & Brazhnikova (1944). The antibiotic acts on the cellular membrane which, in its presence, no longer functions as a penetration barrier for ions.…”

Section: Introductionmentioning

confidence: 99%

Channels in the Gramicidin S-with-Urea Structure and their Possible Relation to Transmembrane Ion Transport

Tishchenko¹,

Andrianov²,

Vainstein³

et al. 1997

Acta Cryst D

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The structure of membrane-active antibiotic cyclodecapeptide gramicidin S in the crystals of its complex with urea, C60H92N12010.0.5[(NH2)2CO ].7.94H20 , has been investigated with three-dimensional X-ray data by the automatic sequential approximation method. The crystals are trigonal, space group P3121, a = 25.80(3), c--21.49(2)A, M r = 7968, calculated density = 1.088mg m -3, Z = 1. Conventional R factor: R1 = 0.0943, wR2 = 0.2478

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“…Gramicidin S (GS) 1 is a cyclic decapeptide that exhibits strong antibiotic activity against a broad spectrum of Gramnegative and Gram-positive bacteria and against several pathogenic fungi (3)(4)(5)(6)(7)(8)(9). Numerous studies by us and others have shown that disruption of the barrier properties of cell membranes is the basis of the antimicrobial and hemolytic properties of GS (3,4,10).…”

mentioning

confidence: 99%

Structure-Activity Relationships of Diastereomeric Lysine Ring Size Analogs of the Antimicrobial Peptide Gramicidin S

Prenner

Kiricsi

Jelokhani-Niaraki

et al. 2005

Journal of Biological Chemistry

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Structure-activity relationships were examined in seven gramicidin S analogs in which the ring-expanded analog GS14 [cyclo-(VKLKVdYPLKVKLdYP)] is modified by enantiomeric inversions of its lysine residues. The conformation, amphiphilicity, and self-association propensity of these peptides were investigated by circular dichroism spectroscopy and reversed phase high performance liquid chromatography. 31 P nuclear magnetic resonance spectroscopic and dye leakage experiments were performed to evaluate the capacity of these peptides to induce inverse nonlamellar phases in, and to permeabilize phospholipid bilayers; their growth inhibitory activity against the cell wall-less mollicute Acholeplasma laidlawii B was also examined. The amount and stability of ␤-sheet structure, effective hydrophobicity, propensity for self-association in water, ability to disrupt the organization of phospholipid bilayers, and ability to inhibit A. laidlawii B growth are strongly correlated with the facial amphiphilicity of these GS14 analogs. Also, the magnitude of the parameters segregate these peptides into three groups, consisting of GS14, the four single inversion analogs, and the two multiple inversion analogs. The capacity of these peptides to differentiate between bacterial and animal cell membranes exhibits a biphasic relationship with peptide amphiphilicity, suggesting that there may only be a narrow range of peptide amphiphilicity within which it is possible to achieve the dual therapeutic requirements of high antibiotic effectiveness and low hemolytic activity. These results were rationalized by considering how the physiochemical properties of these GS14 analogs are likely to be reflected in their partitioning into lipid bilayer membranes.

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Gramicidin S and its use in the Treatment of Infected Wounds

Cited by 266 publications

References 0 publications

Antimicrobial peptides as natural bio-preservative to enhance the shelf-life of food

Antimicrobial peptides as natural bio-preservative to enhance the shelf-life of food

Channels in the Gramicidin S-with-Urea Structure and their Possible Relation to Transmembrane Ion Transport

Structure-Activity Relationships of Diastereomeric Lysine Ring Size Analogs of the Antimicrobial Peptide Gramicidin S

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