Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers

Matsuzaki, Katsumi; Harada, Mitsunori; Funakoshi, Susumu; Fujii, Nobutaka; Miyajima, Koichiro

doi:10.1016/0005-2736(91)90366-g

Cited by 203 publications

(198 citation statements)

References 33 publications

Supporting

Mentioning

184

Contrasting

Order By: Relevance

“…This detergent-like property has been described for other small peptides such as magainins 1 and 2 (Matsuzaki et al, 1989(Matsuzaki et al, , 1991, dermaseptin (Pouny et al, 1992), or melittin (Katsu et al, 1989;Benachir & Lafleur, 1995) and larger proteins like the bacterial toxin a-haemolysin secreted by Escherichia coli (Ostolaza et al, 1993) or CytA, a 27 kDa protein belonging to the family of &endotoxins occumng in parasporal crystals of Bacillus thuringiensis var. israelensis (Butko et al, 1996(Butko et al, , 1997.…”

Section: Mechanism For Membrane Disruptionmentioning

confidence: 71%

Interaction of wheat α‐thionin with large unilamellar vesicles

Caaveiro

Molina

Rodrı́guez-Palenzuela

et al. 1998

Protein Science

View full text Add to dashboard Cite

The interaction of the wheat antibacterial peptide a-thionin with large unilamellar vesicles has been investigated by means of fluorescence spectroscopy. Binding of the peptide to the vesicles is followed by the release of vesicle contents, vesicle aggregation, and lipid mixing. Vesicle fusion, i.e., mixing of the aqueous contents, was not observed. Peptide binding is governed by electrostatic interactions and shows no cooperativity. The amphipatic nature of wheat a-thionin seems to destabilize the membrane bilayer and trigger the aggregation of the vesicles and lipid mixing. The presence of distearoylphosphatidylethanolamine-poly(ethy1ene glycol 2000) (PEG-PE) within the membrane provides a steric barrier that inhibits vesicle aggregation and lipid mixing but does not prevent leakage. Vesicle leakage through discrete membrane channels is unlikely, because the release of encapsulated large fluorescent dextrans is very similar to that of 8-arninonaphthalene-l,3,6,trisulfonic acid (ANTS). A minimum number of 700 peptide molecules must bind to each vesicle to produce complete leakage, which suggests a mechanism in which the overall destabilization of the membrane is due to the formation of transient pores rather than discrete channels.

show abstract

Section: Mechanism For Membrane Disruptionmentioning

confidence: 71%

Interaction of wheat α‐thionin with large unilamellar vesicles

Caaveiro

Molina

Rodrı́guez-Palenzuela

et al. 1998

Protein Science

View full text Add to dashboard Cite

show abstract

“…The baseline (liposomes without peptide) was subtracted. Unilamellar liposomes were prepared as described by Matsuzaki et al [24]. α-Helical content was estimated as described by Greenfield and Fasman [25] and Wu et al [26].…”

Section: Spectramentioning

confidence: 99%

Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide

Saido-Sakanaka

Ishibashi

Sagisaka

et al. 1999

Biochemical Journal

View full text Add to dashboard Cite

Defensin from a beetle, Allomyrina dichotoma, is known to have anti-bacterial activity against Gram-positive bacteria. This peptide, which comprises 43 amino acid residues, was effective against methicillin-resistant Staphylococcus aureus. We identified the active site of beetle defensin by measuring anti-bacterial activity against S. aureus of 64 overlapping 12-mer peptides with either a free carboxylate or a free amide group at their C-termini. An LCAAHCLAIGRR-NH2 (19L–30R-NH2) fragment showed the greatest activity of the synthetic oligopeptides. The 19L–30R-NH2 fragment was effective against both Gram-positive and Gram-negative bacteria. CD spectra showed that the 19L–30R-NH2 fragment formed an α-helical structure in the lipidic environment. The anti-bacterial effect of the 19L–30R-NH2 fragment was due to its interaction with bacterial membranes, judging from the leakage of liposome-entrapped glucose. Its anti-bacterial activity was increased when certain amino acid residues were replaced. Truncated peptides having had some amino acids removed from the N-terminus of the 19L–30R-NH2 fragment (8–10-mer peptides) still had strong anti-bacterial activity. Deleting some amino acids from the C-terminal region of the fragment dramatically reduced activity, indicating that the C-terminal region of the 19L–30R-NH2 fragment, i.e. RR-NH2, is important for exerting anti-bacterial activity. The AHCLAIGRR-NH2 (22A–30R-NH2) fragment and its analogues exhibited about 3-fold and 9–12-fold higher activity against S. aureus than did the 19L–30R-NH2 fragment, and these analogues were effective against methicillin-resistant S. aureus and Pseudomonas aeruginosa isolated from patients. These oligopeptides showed no haemolytic activity and did not inhibit the growth of murine fibroblast cells.

show abstract

“…These linear peptides were shown to be antibacterial, antifungal, and antiprotozoal (17,18). Both types of antimicrobial peptides have been shown to adopt an amphipathic ␣-helical conformation in hydrophobic media (14,19,20). It has been suggested that this structural type of peptide binds anionic phospholipid-rich membranes similar to bacterial membranes and dissolves them like detergents (21)(22)(23).…”

mentioning

confidence: 99%

Isolation and Characterization of Pleurocidin, an Antimicrobial Peptide in the Skin Secretions of Winter Flounder

Cole

Weis

Diamond

1997

Journal of Biological Chemistry

463

301

View full text Add to dashboard Cite

Antimicrobial peptides are found in both myeloid cells and mucosal tissues of many vertebrates and invertebrates. These peptides are predicted to operate as a first-line host defense mechanism exerting broad-spectrum activity against pathogenic bacteria, fungi, parasites, and enveloped viruses. We report the characterization of a novel 25-residue linear antimicrobial peptide found in the skin mucous secretions of the winter flounder (Pleuronectes americanus). This peptide was purified through multiple chromatographic methods to obtain a single peak by reversed-phase high performance liquid chromatography. This purified peptide, which we named pleurocidin, exhibited antimicrobial activity against Escherichia coli in a bacterial cell lysis plate assay. Mass spectrometry and amino acid sequence analysis indicated that it is 25 amino acids in length. Pleurocidin is predicted to assume an amphipathic ␣-helical conformation similar to many other linear antimicrobial peptides. There is a high degree of homology between pleurocidin and two antimicrobial peptides, ceratotoxin from the Mediterranean fruit fly and dermaseptin from the skin of a hylid frog. The minimal inhibitory concentration and minimal bactericidal concentration of pleurocidin were determined against 11 different Gram-negative and Gram-positive bacteria. Immunohistochemistry locates pleurocidin in the epithelial mucous cells of flounder skin. Pleurocidin represents a novel antimicrobial peptide found in fish and may play a role in innate host defense.

show abstract

Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers

Cited by 203 publications

References 33 publications

Interaction of wheat α‐thionin with large unilamellar vesicles

Interaction of wheat α‐thionin with large unilamellar vesicles

Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide

Isolation and Characterization of Pleurocidin, an Antimicrobial Peptide in the Skin Secretions of Winter Flounder

Contact Info

Product

Resources

About