Clavanins and Styelins, α-Helical Antimicrobial Peptides from The Hemocytes of Styela clava

Lehrer, Robert I.; Lee, In Hee; Menzel, Lorenzo P.; Waring, Alan J.; Zhao, Chengquan

doi:10.1007/978-1-4615-1291-2_7

Cited by 23 publications

(20 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Given the pH dependent antimicrobial activity of the peptide, it is tempting to speculate that the ability of Ci-MAM-A24 to kill these various bacterial parasites was potentiated by the low pH of their host cell environments. Clavaspirin, clavanins and styelins were isolated from another solitary tunicate, Styela clava and these pH dependent AMPs were found to be rich in both histidine and phenylalanine residues [68,69]. In general, it was found that clavaspirin and clavanins possessed pH dependent antibacterial and antifungal activity [65,66,67,76] with low pH, enhancing the ability of these AMPs to adopt α-helical structure and permeabilize the membranes of these organisms [68,69].…”

Section: An Overview Of Ph Dependent Peptides and Proteins With Anmentioning

confidence: 99%

“…Clavaspirin, clavanins and styelins were isolated from another solitary tunicate, Styela clava and these pH dependent AMPs were found to be rich in both histidine and phenylalanine residues [68,69]. In general, it was found that clavaspirin and clavanins possessed pH dependent antibacterial and antifungal activity [65,66,67,76] with low pH, enhancing the ability of these AMPs to adopt α-helical structure and permeabilize the membranes of these organisms [68,69]. It appeared that the protonation of histidine residues under low pH conditions promoted the ability of these AMPs to target microbial membranes whilst the presence of their glycine and phenylalanine residues provided them with the conformational flexibility and structural hydrophobicity to facilitate bilayer partitioning [70,71,72,73,74,75].…”

Section: An Overview Of Ph Dependent Peptides and Proteins With Anmentioning

confidence: 99%

See 1 more Smart Citation

pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents

et al. 2016

View full text Add to dashboard Cite

Antimicrobial peptides (AMPs) are potent antibiotics of the innate immune system that have been extensively investigated as a potential solution to the global problem of infectious diseases caused by pathogenic microbes. A group of AMPs that are increasingly being reported are those that utilise pH dependent antimicrobial mechanisms, and here we review research into this area. This review shows that these antimicrobial molecules are produced by a diverse spectrum of creatures, including vertebrates and invertebrates, and are primarily cationic, although a number of anionic examples are known. Some of these molecules exhibit high pH optima for their antimicrobial activity but in most cases, these AMPs show activity against microbes that present low pH optima, which reflects the acidic pH generally found at their sites of action, particularly the skin. The modes of action used by these molecules are based on a number of major structure/function relationships, which include metal ion binding, changes to net charge and conformational plasticity, and primarily involve the protonation of histidine, aspartic acid and glutamic acid residues at low pH. The pH dependent activity of pore forming antimicrobial proteins involves mechanisms that generally differ fundamentally to those used by pH dependent AMPs, which can be described by the carpet, toroidal pore and barrel-stave pore models of membrane interaction. A number of pH dependent AMPs and antimicrobial proteins have been developed for medical purposes and have successfully completed clinical trials, including kappacins, LL-37, histatins and lactoferrin, along with a number of their derivatives. Major examples of the therapeutic application of these antimicrobial molecules include wound healing as well as the treatment of multiple cancers and infections due to viruses, bacteria and fungi. In general, these applications involve topical administration, such as the use of mouth washes, cream formulations and hydrogel delivery systems. Nonetheless, many pH dependent AMPs and antimicrobial proteins have yet to be fully characterized and these molecules, as a whole, represent an untapped source of novel biologically active agents that could aid fulfillment of the urgent need for alternatives to conventional antibiotics, helping to avert a return to the pre-antibiotic era.

show abstract

Section: An Overview Of Ph Dependent Peptides and Proteins With Anmentioning

confidence: 99%

Section: An Overview Of Ph Dependent Peptides and Proteins With Anmentioning

confidence: 99%

pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents

et al. 2016

View full text Add to dashboard Cite

show abstract

“…These peptides exhibit broad-spectrum antimicrobial activities against Gram-positive and Gramnegative bacteria, as well as several fungi (1,2). Similar to many other naturally occurring peptide antibiotics (4)(5)(6)(7)(8)(9)(10), the clavanins exert their antimicrobial effect via permeabilization of the target membranes (11)(12)(13).…”

mentioning

confidence: 99%

The Peptide Antibiotic Clavanin A Interacts Strongly and Specifically with Lipid Bilayers

et al. 2003

View full text Add to dashboard Cite

In this study the interaction of the antimicrobial peptide clavanin A with phosphatidylcholine bilayers is investigated by DSC, NMR, and AFM techniques. It is shown that the peptide interacts strongly and specifically with the lipids, resulting in increased order-disorder phase transition temperatures, phase separation, altered acyl chain and headgroup packing, and a drastically changed surface morphology of the bilayer. These results are interpreted in terms of clavanin-specific interactions with lipids and are discussed in the light of the different mechanisms by which clavanin A can destroy the barrier function of biological membranes.

show abstract

“…Extraction was carried out according to Lehrer et al [16][17][18][19] . At first, Whole body (except viscera) was ground into fine powder in the liquid nitrogen.…”

Section: Extractionmentioning

confidence: 99%

Antibacterial and molecular dynamics study of the Dolabellanin B2 isolated from sea slug, Peronia peronii

Bitaab¹,

Siadat²,

Pazooki³

et al. 2015

Biosci., Biotech. Res. Asia

View full text Add to dashboard Cite

Marine gastropod, Peronia peronei, from north of the Persian Gulf, protein extraction was investigated using ultrafiltration, reversed-phase high-performance liquid chromatography and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/TOF). The mass spectra showed that, the isolated peptide is most probably Dolabellanin B2 that has been extracted before from other marine mollusk, Dolabella auricularia. The antibacterial activity of purified peptide was assessed against seven bacterial strains (Staphylococcus aureus, Bacillus subtilis, Serratia marcescens, Escherichia coli, Klebsiella pneumoniae, Pseudomonas aeruginosa and Proteus mirabilis). Broth micro-dilution method, standard disk diffusion assay and bioautography were used for this aim. According to the results the identified peptide showed strong antibacterial activity against all mentioned bacterial strains. Computational studies through peptide modeling servers followed by 50 ns molecular dynamics simulation and surface electrostatic calculations indicates that this sequence could be most probably related to alpha helical cationic antimicrobial peptides (alpha-CAMPs) with overall charge of +1 at pH 7.

show abstract

Clavanins and Styelins, α-Helical Antimicrobial Peptides from The Hemocytes of Styela clava

Cited by 23 publications

References 6 publications

pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents

pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents

The Peptide Antibiotic Clavanin A Interacts Strongly and Specifically with Lipid Bilayers

Antibacterial and molecular dynamics study of the Dolabellanin B2 isolated from sea slug, Peronia peronii

Contact Info

Product

Resources

About