Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
Biochem J
2001 Oct 01;359Pt 1:35-45. doi: 10.1042/0264-6021:3590035.
Show Gene links
Show Anatomy links
Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator.
Corzo G
,
Escoubas P
,
Villegas E
,
Barnham KJ
,
He W
,
Norton RS
,
Nakajima T
.
???displayArticle.abstract???
Two novel antimicrobial peptides have been identified and characterized from venom of the African scorpion Pandinus imperator. The peptides, designated pandinin 1 and 2, are alpha-helical polycationic peptides, with pandinin 1 belonging to the group of antibacterial peptides previously described from scorpions, frogs and insects, and pandinin 2 to the group of short magainin-type helical peptides from frogs. Both peptides demonstrated high antimicrobial activity against a range of Gram-positive bacteria (2.4-5.2 microM), but were less active against Gram-negative bacteria (2.4-38.2 microM), and only pandinin 2 affected the yeast Candida albicans. Pandinin 2 also demonstrated strong haemolytic activity (11.1-44.5 microM) against sheep erythrocytes, in contrast with pandinin 1, which was not haemolytic. CD studies and a high-resolution structure of pandinin 2 determined by NMR, showed that the two peptides are both essentially helical, but differ in their overall structure. Pandinin 2 is composed of a single alpha-helix with a predominantly hydrophobic N-terminal sequence, whereas pandinin 1 consists of two distinct alpha-helices separated by a coil region of higher flexibility. This is the first report of magainin-type polycationic antimicrobial peptides in scorpion venom. Their presence brings new insights into the mode of action of scorpion venom and also opens new avenues for the discovery of novel antibiotic molecules from arthropod venoms.
Batista,
Antimicrobial peptides from the Brazilian frog Phyllomedusa distincta.
1999, Pubmed
Batista,
Antimicrobial peptides from the Brazilian frog Phyllomedusa distincta.
1999,
Pubmed
Bazzo,
The structure of melittin. A 1H-NMR study in methanol.
1988,
Pubmed
Bechinger,
Towards membrane protein design: pH-sensitive topology of histidine-containing polypeptides.
1996,
Pubmed
Bechinger,
The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy.
1999,
Pubmed
,
Xenbase
Böhm,
Quantitative analysis of protein far UV circular dichroism spectra by neural networks.
1992,
Pubmed
Bulet,
Antimicrobial peptides in insects; structure and function.
1999,
Pubmed
Cociancich,
Purification and characterization of a scorpion defensin, a 4kDa antibacterial peptide presenting structural similarities with insect defensins and scorpion toxins.
1993,
Pubmed
Conde,
Scorpine, an anti-malaria and anti-bacterial agent purified from scorpion venom.
2000,
Pubmed
Csordás,
Primary structure of two oligopeptides of the toxin of Bombina variegata L.
1969,
Pubmed
Daly,
Frog secretions and hunting magic in the upper Amazon: identification of a peptide that interacts with an adenosine receptor.
1992,
Pubmed
Dathe,
Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells.
1999,
Pubmed
,
Xenbase
Dempsey,
Contribution of proline-14 to the structure and actions of melittin.
1991,
Pubmed
Ehret-Sabatier,
Characterization of novel cysteine-rich antimicrobial peptides from scorpion blood.
1996,
Pubmed
Fennell,
Antibacterial action of melittin, a polypeptide from bee venom.
1968,
Pubmed
Gesell,
Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution.
1997,
Pubmed
,
Xenbase
Güntert,
Torsion angle dynamics for NMR structure calculation with the new program DYANA.
1997,
Pubmed
Habermann,
[Sequence analysis of melittin from tryptic and peptic degradation products].
1967,
Pubmed
Haeberli,
Characterisation of antibacterial activity of peptides isolated from the venom of the spider Cupiennius salei (Araneae: Ctenidae).
2000,
Pubmed
Hancock,
Cationic peptides: a new source of antibiotics.
1998,
Pubmed
Hoffmann,
Phylogenetic perspectives in innate immunity.
1999,
Pubmed
Holak,
The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study.
1988,
Pubmed
Hwang,
Structure-function relationships of antimicrobial peptides.
1998,
Pubmed
Iwai,
Solution conformation of an antibacterial peptide, sarcotoxin IA, as determined by 1H-NMR.
1993,
Pubmed
Iwanaga,
New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions.
1998,
Pubmed
Koradi,
MOLMOL: a program for display and analysis of macromolecular structures.
1996,
Pubmed
Lee,
Antimicrobial activity and conformation of gaegurin-6 amide and its analogs.
1998,
Pubmed
Ludtke,
Membrane pores induced by magainin.
1996,
Pubmed
,
Xenbase
Morikawa,
Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa.
1992,
Pubmed
,
Xenbase
Nicolas,
Peptides as weapons against microorganisms in the chemical defense system of vertebrates.
1995,
Pubmed
Okada,
Primary structure of sarcotoxin I, an antibacterial protein induced in the hemolymph of Sarcophaga peregrina (flesh fly) larvae.
1985,
Pubmed
Pallaghy,
Solution structure of robustoxin, the lethal neurotoxin from the funnel-web spider Atrax robustus.
1997,
Pubmed
Park,
Antimicrobial peptides from the skin of a Korean frog, Rana rugosa.
1994,
Pubmed
Shai,
Molecular recognition between membrane-spanning polypeptides.
1995,
Pubmed
Sharon,
2D-NMR and ATR-FTIR study of the structure of a cell-selective diastereomer of melittin and its orientation in phospholipids.
1999,
Pubmed
Silva,
Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family.
2000,
Pubmed
Simmaco,
Novel antimicrobial peptides from skin secretion of the European frog Rana esculenta.
1993,
Pubmed
Simmaco,
Temporins, antimicrobial peptides from the European red frog Rana temporaria.
1996,
Pubmed
Sitaram,
Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity.
1999,
Pubmed
Sönnichsen,
Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide.
1992,
Pubmed
Srisailam,
Conformational study of a custom antibacterial peptide cecropin B1: implications of the lytic activity.
2000,
Pubmed
Steiner,
Sequence and specificity of two antibacterial proteins involved in insect immunity.
1981,
Pubmed
Torres-Larios,
Hadrurin, a new antimicrobial peptide from the venom of the scorpion Hadrurus aztecus.
2000,
Pubmed
Vogt,
The interactions of histidine-containing amphipathic helical peptide antibiotics with lipid bilayers. The effects of charges and pH.
1999,
Pubmed
Wishart,
1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects.
1995,
Pubmed
Wong,
The solution structure and activity of caerin 1.1, an antimicrobial peptide from the Australian green tree frog, Litoria splendida.
1997,
Pubmed
Yan,
Lycotoxins, antimicrobial peptides from venom of the wolf spider Lycosa carolinensis.
1998,
Pubmed
Zasloff,
Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.
1987,
Pubmed
,
Xenbase
