Amphibian skin: A promising resource for antimicrobial peptides

Barra, Donatella; Simmaco, Maurizio

doi:10.1016/s0167-7799(00)88947-7

Cited by 260 publications

(202 citation statements)

References 32 publications

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“…1F), with the fluctuating levels between 2 and 4 nA. The strong interaction between negatively charged phospholipid head-groups and cationic residues is an important step in membrane permeation of antimicrobial peptides from amphibian skin (1)(2)(3)(4). To test the eventual role of negatively charged lipids on D1 properties, other experiments were performed into phosphatidylcholine͞phosphatidylethanolamine͞ phosphatidylserine bilayers at various voltages.…”

Section: Resultsmentioning

confidence: 99%

“…Frogs and toads are known to secrete from dorsal granular glands two main classes of these compounds (1)(2)(3)(4). The first group includes linear peptides with no cysteines that form an amphipathic ␣-helical structure in hydrophobic environment (1)(2)(3)(4)(5).…”

mentioning

confidence: 99%

“…The first group includes linear peptides with no cysteines that form an amphipathic ␣-helical structure in hydrophobic environment (1)(2)(3)(4)(5). The second class comprises peptides presenting a Cterminal S-S bridge, which generates a 7-to 9-aa cyclic moiety (1,4). Recently, different antimicrobial molecules with intriguing structural features have been discovered (6).…”

mentioning

confidence: 99%

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A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin

Raimondo

Andreotti

Saint

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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Many bioactive peptides, presenting an unstructured conformation in aqueous solution, are made resistant to degradation by posttranslational modifications. Here, we describe how molecular oligomerization in aqueous solution can generate a still unknown transport form for amphipathic peptides, which is more compact and resistant to proteases than forms related to any possible monomer. This phenomenon emerged from 3D structure, function, and degradation properties of distinctin, a heterodimeric antimicrobial compound consisting of two peptide chains linked by a disulfide bond. After homodimerization in water, this peptide exhibited a fold consisting of a symmetrical full-parallel four-helix bundle, with a well secluded hydrophobic core and exposed basic residues. This fold significantly stabilizes distinctin against proteases compared with other linear amphipathic peptides, without affecting its antimicrobial, hemolytic, and ion-channel formation properties after membrane interaction. This full-parallel helical orientation represents a perfect compromise between formation of a stable structure in water and requirement of a drastic structural rearrangement in membranes to elicit antimicrobial potential. Thus, distinctin can be claimed as a prototype of a previously unrecognized class of antimicrobial derivatives. These results suggest a critical revision of the role of peptide oligomerization whenever solubility or resistance to proteases is known to affect biological properties.NMR structure ͉ oligomerization ͉ pore-forming peptide ͉ disulfide

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin

Raimondo

Andreotti

Saint

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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“…Once stimulated, secretions produced within the cell discharge by the rupture of the plasma membrane, thus releasing the cellular contents into the lumen. AMPs stored in the granular glands in prepropeptide form will remove the signal peptide from the precursor and release into the skin surface in a holocrine manner upon stress and injury (37,38).…”

Section: Expression and Post-translational Modifications Of Amphibianmentioning

confidence: 99%

Antimicrobial peptides from amphibians

Xiao

Liu

Lai

2011

BioMolecular Concepts

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Increased prevalence of multi-drug resistance in pathogens has encouraged researchers to focus on finding novel forms of anti-infective agents. Antimicrobial peptides (AMPs) found in animal secretions are components of host innate immune response and have survived eons of pathogen evolution. Thus, they are likely to be active against pathogens and even those that are resistant to conventional drugs. Many peptides have been isolated and shown to be effective against multi-drug resistant pathogens. More than 500 AMPs have been identified from amphibians. The abundance of AMPs in frog skin is remarkable and constitutes a rich source for design of novel pharmaceutical molecules. Expression and post-translational modifications, discovery, activities and probable therapeutic application prospects of amphibian AMPs will be discussed in this article.

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“…Ever since magainin was discovered from African clawed frog, Xenopus laevis, quite a number of antimicrobial peptides were discovered subsequently in other frog species such as Ranidae [10]. In 1992-1994, for example, a novel family of antimicrobial peptides, brevinins [33,37], esculentins [34], ranalexin [13], and gaegurins [25] have been detected in the skin of Rana brevipoda, Rana esculenta, Rana catesbeiana, and Rana rugosa, frogs of the family of Ranidae, respectively.…”

Section: Introductionmentioning

confidence: 99%

Structural studies on the antimicrobial peptide Brevinin 1E by spectroscopic methods

Son¹,

Kim²,

Kim³

et al. 2003

Spectroscopy

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Abstract. Skin extracts of frogs are a rich source of pharmacologically active peptides such as caeruleins, tachykinins, bradykinins, thyrotropin-releasing hormone, bombesin-like and opioid peptides. A large variety of antimicrobial peptides has been isolated from Rana species. These peptides, grouped in several families on the basis of differing length and distinct activity, were found to have one structural motif in common: an intramolecular disulfide bridge located at the C-terminal end, forming a seven-member ring, which was designated 'Rana box'. Brevinin 1E is a 24-residue antimicrobial peptide isolated from the skin of a frog, Rana brevipoda. This peptide shows a broad range of antimicrobial activity against prokaryotic cells but shows very much hemolytic activity against human red blood cells. The solution structure of Brevinin 1E was studied by using CD (circular dichroism) and NMR (nuclear magnetic resonance) spectroscopy. CD investigation revealed that Brevinin 1E adopts random structure in aqueous solution but adopts mainly α-helical structure in TFE/water (6 : 4, v/v) solution. The three-dimensional structure of Brevinin 1E was determined in 60% TFE/water solution using homonuclear NMR spectroscopy. This peptide showed mainly an α-helical structure with amphipathic property. Its three-dimensional structure is similar to those of other peptides such as magainin, nigrocin and ranalexin. Therefore, Brevinin 1E can be classified into the family of antimicrobial peptides containing a single linear α-helix that interact with target microbial membrane, leading to cell death through disruption of membrane integrity.

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Amphibian skin: A promising resource for antimicrobial peptides

Cited by 260 publications

References 32 publications

A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin

A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin

Antimicrobial peptides from amphibians

Structural studies on the antimicrobial peptide Brevinin 1E by spectroscopic methods

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