Animal antimicrobial peptides: An overview

Andreu, David; Rivas, Luís

doi:10.1002/(sici)1097-0282(1998)47:6<415::aid-bip2>3.0.co;2-d

Cited by 569 publications

(453 citation statements)

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“…3,4 Extensive studies on the mechanism of the antibacterial action of defensins have revealed that electrostatic interactions occur initially between the cationic peptides and the negatively charged bacterial membrane components, followed by peptide insertion, channel formation and disruption of membranes. 5 Because of the presence of cholesterol and mostly zwitterinic phospholipids on eukaryotic membranes, AMPs are generally much less lytic to eukaryotic cells, with the antibacterial concentrations being mostly 10-to 100-fold lower than cytotoxical concentrations.…”

Section: Introductionmentioning

confidence: 99%

In vitro antibacterial and hemolytic activities of crotamine, a small basic myotoxin from rattlesnake Crotalus durissus

et al. 2011

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Crotamine, a myotoxin from the venom of South American rattlesnake, is structurally related to b-defensins, antimicrobial peptides (AMPs) found in vertebrate animals. Here, we tested the antibacterial properties of crotamine and found that it killed several strains of Escherichia coli, with the MICs ranging from 25 to 100 lg ml À1 . Time-kill and bacterial membrane permeabilization assays revealed that killing of bacteria by crotamine occurred within 1 h and reached the maximum by 2 h. Additionally, the anti-E. coli activity of crotamine was completely abolished with 12.5 mM NaCl. Furthermore, the three intramolecular disulfide bonds of crotamine appeared dispensable for its antibacterial activity. The reduced form of crotamine was active against E. coli as well. However, crotamine showed no or weak activity up to 200 lg ml À1 against other species of Gram-negative and Gram-positive bacteria. Crotamine showed no appreciable hemolytic activity to erythrocytes. Our studies revealed that crotamine is also an AMP that kills bacteria through membrane permeabilization. However, crotamine appears to have a narrow antibacterial spectrum, distinct from many classical b-defensins, reinforcing the notion that crotamine originated from the b-defensin gene lineage, but has undergone significant functional diversification.

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Section: Introductionmentioning

confidence: 99%

In vitro antibacterial and hemolytic activities of crotamine, a small basic myotoxin from rattlesnake Crotalus durissus

et al. 2011

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“…5 Cecropin A (CA) and melittin (M) provided the first examples of EAP sequence hybridization. [6][7][8] CA(1-8)M (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18), one of the most successful examples of the hybridization concept, showed improved antimicrobial activity relative to parent cecropin A and greatly reduced the hemolytic properties of melittin. Taking CA(1-8)M(1-18) as lead, a subsequent approach was to further reduce the size of the hybrid CA-M peptides while retaining antimicrobial activity.…”

Section: Introductionmentioning

confidence: 99%

“…Taking CA(1-8)M(1-18) as lead, a subsequent approach was to further reduce the size of the hybrid CA-M peptides while retaining antimicrobial activity. This led to CA-(1-7)M(2-9), 9 a pentadecapeptide that preserves most of the activity of CA(1-8)M (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18).…”

Section: Introductionmentioning

confidence: 99%

“…16 Other investigations on microorganisms confirmed that, generally, antimicrobial peptides exert their activity by permeabilizing the plasma membrane. 3,11,17,18 Alternative mechanisms of action have been proposed for some antimicrobial peptides, 4,[19][20][21][22][23][24][25][26][27][28] and the requirements for peptide antimicrobial activity have also been extensively discussed. 3,[29][30][31][32][33] Differential scanning calorimetry (DSC) has emerged as a most valuable tool to study peptide-membrane interactions.…”

Section: Introductionmentioning

confidence: 99%

“…3,11,17,18 Alternative mechanisms of action have been proposed for some antimicrobial peptides, 4,[19][20][21][22][23][24][25][26][27][28] and the requirements for peptide antimicrobial activity have also been extensively discussed. 3,[29][30][31][32][33] Differential scanning calorimetry (DSC) has emerged as a most valuable tool to study peptide-membrane interactions. 28,30,[34][35][36][37][38][39] DSC analysis provides a thermodynamic characterization of the changes induced by peptides on liposome phase transitions.…”

Section: Introductionmentioning

confidence: 99%

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Interaction and Lipid-Induced Conformation of Two Cecropin−Melittin Hybrid Peptides Depend on Peptide and Membrane Composition

et al. 2005

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The interaction of two hybrid peptides of cecropin A and melittin [CA(1-8)M(1-18) and CA(1-7)M(2-9)] with liposomes was studied by differential scanning calorimetry (DSC), circular dichroism (CD), and quasi-elastic light scattering (QELS). The study was carried out with large unilamellar vesicles (LUVs) of three different lipid compositions: 1,2-dimyristoil-sn-glycero-3-phosphocholine (DMPC), 1,2-dimyristoylsn-glycero-3-phospho-rac-(1-glycerol) (DMPG) and a binary mixture of DMPC/DMPG, in a wide range of peptide-to-lipid (P:L) molar ratios (0 to 1:7). DSC results indicate that, for both peptides, the interaction depends on membrane composition, with very different behavior for zwitterionic and anionic membranes. CD data show that, although the two peptides have different secondary structures in buffer (random coil for CA(1-7)M(2-9) and predominantly -sheet for CA(1-8)M(1-18)), they both adopt an R-helical structure in the presence of the membranes. Overall, results are compatible with a model involving a strong electrostatic surface interaction between the peptides and the negatively charged liposomes, which gives place to aggregation in the gel phase and precipitation after a threshold peptide concentration. In the case of zwitterionic membranes, a progressive surface coverage with peptide molecules destabilizes the membrane, eventually leading to membrane disruption. Moreover, delicate modulations in behavior were observed depending on the peptide.

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