Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis

Konno, Katsuhiro; Hisada, Miki; Fontana, Renato; Lorenzi, Carla C. B.; Naoki, Hideo; Itagaki, Yasuhiro; Miwa, Akiko; Kawai, Nobufumi; Nakata, Yoshihiro; Yasuhara, Tadashi; Neto, João Ruggiero; Azevedo, Walter Filgueira de; Palma, Mário Sérgio; Nakajima, Terumi

doi:10.1016/s0167-4838(01)00271-0

Cited by 147 publications

(148 citation statements)

References 38 publications

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“…In the solitary wasp case, some of the AMPs found in the venom may play a role in the prevention of potential infections due to prey ingestion. [26] We speculate that the primary role of MEP in the venom may be in protecting the solitary bee against enemies, with the antimicrobial role more or less secondary.…”

Section: Discussionmentioning

confidence: 92%

Melectin: A Novel Antimicrobial Peptide from the Venom of the Cleptoparasitic Bee Melecta albifrons

et al. 2008

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A novel antimicrobial peptide designated melectin was isolated from the venom of the cleptoparasitic bee Melecta albifrons. Its primary sequence was established as H-Gly-Phe-Leu-Ser-Ile-Leu-Lys-Lys-Val-Leu-Pro-Lys-Val-Met-Ala-His-Met-Lys-NH(2) by Edman degradation and ESI-QTOF mass spectrometry. Synthetic melectin exhibited antimicrobial activity against both gram-positive and -negative bacteria and it degranulated rat peritoneal mast cells, but its hemolytic activity was low. The CD spectra of melectin measured in the presence of trifluoroethanol and sodium dodecyl sulfate showed a high content alpha-helices, which indicates that melectin can adopt an amphipathic alpha-helical secondary structure in an anisotropic environment such as the bacterial cell membrane. To envisage the role of the proline residue located in the middle of the peptide chain on biological activity and secondary structure, we prepared several melectin analogues in which the Pro11 residue was either replaced by other amino acid residues or was omitted. The results of biological testing suggest that a Pro kink in the alpha-helical structure of melectin plays an important role in selectivity for bacterial cells. In addition, a series of N- and C-terminal-shortened analogues was synthesized to examine which region of the peptide is related to antimicrobial activity.

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Section: Discussionmentioning

confidence: 92%

Melectin: A Novel Antimicrobial Peptide from the Venom of the Cleptoparasitic Bee Melecta albifrons

et al. 2008

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“…The mast cells were obtained from the peritoneal fluid of male, 11-week-old rats (Wistar, Clea Japan). Tyrode's-Hepes solution (NaCl 137 mM, KCl 2.7 mM, CaCl 2 1.8 mM, MgCl 2 …”

Section: Methodsmentioning

confidence: 99%

“…Cytotoxic peptides are relatively small cationic molecules found in venoms (1)(2)(3)(4)(5), blood (6,7), tissue surface secretions (8 -10), or even as autocytotoxicity peptides (11) from a broad range of organisms. They interact with lipid bilayers resulting in an alteration of the membrane permeability of the cells through the formation of new ion channels in the cell membrane and/or by changing the activity of existing channels (12,13).…”

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confidence: 99%

IsCT, a Novel Cytotoxic Linear Peptide from Scorpion Opisthacanthus madagascariensis

Dai

Yasuda

Naoki

et al. 2001

Biochemical and Biophysical Research Communications

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109

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“…Scans between 290 nm and 190 nm, with an average of five scans per experiment were averaged from recording in a 0.1-cm cell. Following baseline correction, the percentage a-helicity of the peptides was determined as described by Konno et al (2001) and McLean et al (1991). Small unilamellar vesicles (SUVs) were prepared as described by Gad et al (E.A.…”

Section: Spectroscopymentioning

confidence: 99%

Structure–activity study of the antibacterial peptide fallaxin

et al. 2007

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Fallaxin is a 25-mer antibacterial peptide amide, which was recently isolated from the West Indian mountain chicken frog Leptodactylus fallax. Fallaxin has been shown to inhibit the growth of several Gram-negative bacteria including Enterobacter cloacae, Escherichia coli, Klebsiella pneumoniae, and Pseudomonas aeruginosa. Here, we report a structure-activity study of fallaxin based on 65 analogs, including a complete alanine scan and a full set of N-and C-terminal truncated analogs. The fallaxin analogs were tested for hemolytic activity and antibacterial activity against methicillin-resistant Staphylococcus aureus (MRSA), vancomycin-intermediate resistant S. aureus, (VISA), methicillinsusceptible S. aureus (MSSA), E. coli, K. pneumoniae, and P. aeruginosa. We identified several analogs, which showed improved antibacterial activity compared to fallaxin. Our best candidate was FA12, which displayed MIC values of 3.12, 25, 25, and 50 mM against E. coli, K. pneumoniae, MSSA, and VISA, respectively. Furthermore, we correlated the antibacterial activity with various structural parameters such as charge, hydrophobicity AEHae, mean hydrophobic moment AEm H ae, and a-helicity. We were able to group the active and inactive analogs according to mean hydrophobicity AEHae and mean hydrophobic moment AEm H ae. Far-UV CD-spectroscopy experiments on fallaxin and several analogs in buffer, in TFE, and in membrane mimetic environments (small unilamellar vesicles) indicated that a coiled-coil conformation could be an important structural trait for antibacterial activity. This study provides data that support fallaxin analogs as promising lead structures in the development of new antibacterial agents.Keywords: alanine scan; antibacterial activity; coiled-coil conformation; fallaxin; solid-phase peptide synthesis Reprint requests to: Paul Robert Hansen, Department of Natural Sciences, Faculty of Life Sciences, University of Copenhagen, 1871 Frederiksberg C, Denmark; e-mail: prh@life.ku.dk; fax: 45-35332398.Abbreviations: ACTH, adrenocorticotropic hormone; ATCC, American type culture collection; Boc, tert-butyloxycarbonyl; BSA: bovine serum albumin; CFU, colony forming unit; CPD, citrate-phosphatedextrose; DIEA, diisopropylethylamine; DMPC, 1,2-dimyristoyl-snglycero-3-phosphocholine; DMPG, 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol; DTT: dithiothrethiol; Fmoc: 9-fluorenylmethoxy; AEHae, mean hydrophobicity; HC 50 : the toxin concentration yielding 50% lysis of a 1% suspension of erythrocytes after 45 min at 37°C; AEm H ae, mean hydrophobic moment; HATU, (2-(7-Aza-1H-benzotriazole-1-yl)-1,1,3,3-tetramethyluronium hexafluorophosphate); HOBt, 1-hydroxybenzotriazole; MALDI-TOF MS, matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry; MIC, minimum inhibitory concentration; NMP, N-methyl-2-pyrrolidone; SUV, small unilamellar vesicles; TFA, trifluoroacetic acid; TFE, trifluoroethanol; TIS, triisopropylsilane; Trt, triphenylmethyl.Article and publication are at

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Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis

Cited by 147 publications

References 38 publications

Melectin: A Novel Antimicrobial Peptide from the Venom of the Cleptoparasitic Bee Melecta albifrons

Melectin: A Novel Antimicrobial Peptide from the Venom of the Cleptoparasitic Bee Melecta albifrons

IsCT, a Novel Cytotoxic Linear Peptide from Scorpion Opisthacanthus madagascariensis

Structure–activity study of the antibacterial peptide fallaxin

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