Decoralin, a novel linear cationic α-helical peptide from the venom of the solitary eumenine wasp Oreumenes decoratus

Konno, Katsuhiro; Rangel, Marisa; Oliveira, João Samuel Meira de; Cabrera, Marcia Perez dos Santos; Fontana, Renato; Hirata, Izaura Yoshico; Hide, Izumi; Nakata, Yoshihiro; Mori, Kentaro; Kawano, Marii; Fuchino, Hiroyuki; Sekita, Setsuko; Neto, João Ruggiero

doi:10.1016/j.peptides.2007.09.017

Cited by 80 publications

(79 citation statements)

References 31 publications

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“…C-terminal amidation is typical for the AMPs belonging to the category of linear amphipathic a-helical peptides. The terminal -CONH 2 group provides an extra hydrogen bond that stabilizes the C-terminal end of a-helical structure (Konno et al 2007) and neutralizes the C-terminal negative charge, resulting together in enhanced antimicrobial activity (Č eřovský et al 2008a;Kim et al 2011). In this work, we showed that the C-terminally amidated lasiocepsin analog (lasiocepsin-NH 2 ) also exhibited slightly improved antimicrobial activity, especially against E. coli and S. aureus compared to non-amidated lasiocepsin.…”

Section: Discussionmentioning

confidence: 74%

Lasiocepsin, a novel cyclic antimicrobial peptide from the venom of eusocial bee Lasioglossum laticeps (Hymenoptera: Halictidae)

et al. 2011

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In the venom of eusocial bee Lasioglossum laticeps, we identified a novel unique antimicrobial peptide named lasiocepsin consisting of 27 amino acid residues and two disulfide bridges. After identifying its primary structure, we synthesized lasiocepsin by solid-phase peptide synthesis using two different approaches for oxidative folding. The oxidative folding of fully deprotected linear peptide resulted in a mixture of three products differing in the pattern of disulfide bridges. Regioselective disulfide bond formation significantly improved the yield of desired product. The synthetic lasiocepsin possessed antimicrobial activity against both Gram-positive and -negative bacteria, antifungal activity against Candida albicans, and no hemolytic activity against human erythrocytes. We synthesized two lasiocepsin analogs cyclized through one native disulfide bridge in different positions and having the remaining two cysteines substituted by alanines. The analog cyclized through a Cys8-Cys25 disulfide bridge showed reduced antimicrobial activity compared to the native peptide while the second one (Cys17-Cys27) was almost inactive. Linear lasiocepsin having all four cysteine residues substituted by alanines or alkylated was also inactive. That was in contrast to the linear lasiocepsin with all four cysteine residues non-paired, which exhibited remarkable antimicrobial activity. The shortening of lasiocepsin by several amino acid residues either from the N- or C-terminal resulted in significant loss of antimicrobial activity. Study of Bacillus subtilis cells treated by lasiocepsin using transmission electron microscopy showed leakage of bacterial content mainly from the holes localized at the ends of the bacterial cells.

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Section: Discussionmentioning

confidence: 74%

Lasiocepsin, a novel cyclic antimicrobial peptide from the venom of eusocial bee Lasioglossum laticeps (Hymenoptera: Halictidae)

et al. 2011

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“…Amidation of the C-terminal carboxyl increases antimicrobial activity It has been shown that amidation of the C-terminal carboxyl group is able to improve the antimicrobial activity of AMPs (Falla et al, 1996;Oren and Shai, 1996;Jia et al, 2000;Konno et al, 2007). When the structures of the AMP dermaseptin S3 and its amidated analog were compared, Shalev et al found that the amidated dermaseptin has an induced and/or stabilized α-helical conformation, and thus, is more rigid and extended than the nonamidated analog (Shalev et al, 2002).…”

Section: Part IImentioning

confidence: 99%

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

2010

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Antimicrobial peptides (AMPs), with their extraordinary properties, such as broad-spectrum activity, rapid action and difficult development of resistance, have become promising molecules as new antibiotics. Despite their various mechanisms of action, the interaction of AMPs with the bacterial cell membrane is the key step for their mode of action. Moreover, it is generally accepted that the membrane is the primary target of most AMPs, and the interaction between AMPs and eukaryotic cell membranes (causing toxicity to host cells) limits their clinical application. Therefore, researchers are engaged in reforming or de novo designing AMPs as a 'singleedged sword' that contains high antimicrobial activity yet low cytotoxicity against eukaryotic cells. To improve the antimicrobial activity of AMPs, the relationship between the structure and function of AMPs has been rigorously pursued. In this review, we focus on the current knowledge of α-helical cationic antimicrobial peptides, one of the most common types of AMPs in nature.

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“…Our computational method requires at least one template sequence as a reference. We investigated the membranolytic effects and membrane selectivities of two such templates: protonectin (ILGTILGLLKGL NH 2 ) [22,23] and decoralin (SLLSLIRKLIT NH 2 ), [24] two cationic AMPs from wasp venom. By computational design and residue permutation we generated variations of the template sequences and analyzed their effects with the aid of model lipid vesicles as membrane surrogates, surface plasmon resonance (SPR), isothermal titration calorimetry (ITC), circular dichroism (CD) spectroscopic measurements, and bacterial growth assays.…”

mentioning

confidence: 99%

Piloting the Membranolytic Activities of Peptides with a Self‐organizing Map

Lin¹,

Hiss²,

Schneider³

et al. 2014

ChemBioChem

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Antimicrobial peptides (AMPs) show remarkable selectivity toward lipid membranes and possess promising antibiotic potential. Their modes of action are diverse and not fully understood, and innovative peptide design strategies are needed to generate AMPs with improved properties. We present a de novo peptide design approach that resulted in new AMPs possessing low-nanomolar membranolytic activities. Thermal analysis revealed an entropy-driven mechanism of action. The study demonstrates sustained potential of advanced computational methods for designing peptides with the desired activity.

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Decoralin, a novel linear cationic α-helical peptide from the venom of the solitary eumenine wasp Oreumenes decoratus

Cited by 80 publications

References 31 publications

Lasiocepsin, a novel cyclic antimicrobial peptide from the venom of eusocial bee Lasioglossum laticeps (Hymenoptera: Halictidae)

Lasiocepsin, a novel cyclic antimicrobial peptide from the venom of eusocial bee Lasioglossum laticeps (Hymenoptera: Halictidae)

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

Piloting the Membranolytic Activities of Peptides with a Self‐organizing Map

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