Solution structure of termite-derived antimicrobial peptide, spinigerin, as determined in SDS micelle by NMR spectroscopy

Lee, Kwang Hwan; Shin, Song Yub; Hong, Jung Eun; Yang, Seun-Ah; Kim, Jae Il; Hahm, Kyung‐Soo; Kim, Yangmee

doi:10.1016/j.bbrc.2003.08.043

Cited by 27 publications

(14 citation statements)

References 17 publications

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“…Omitting the slight curvature, this structure, built on the basis of 542 NOEs, is rather similar to the one previously determined in SDS micelles with only 232 NOEs. 21 However, the last model seems well defined, primarily because of the introduction of an unexpected high number of -angle restraints (23 for a 25-residue peptide) in the calculation. But this model is not deposited in the Protein Data Bank, which prevents further comparisons.…”

Section: Discussionmentioning

confidence: 99%

“…A best-fit superposition of the 10 models shows that spini50 adopts a well-defined -helical conformation from Lys4 to Thr23 (Figure 4B), comparable to the structure obtained in SDS micelles. 21 The pairwise RMS deviation, calculated on all C coordinates of the peptide, is 1.80 6 0.46 Å , while it is only 0.90 6 0.35 Å for the segment Lys4-Thr23. However, MOL-MOL and PROCHECK analysis demonstrate that the -helix is not uniformly formed over the peptide.…”

Section: Nuclear Magnetic Resonance and Structure Calculationsmentioning

confidence: 99%

“…Its 3D structure has already been determined in sodium dodecyl sulfate (SDS) micelles. 21 This peptide is rather effective on filamentous fungi and yeast cells (MIC < 5 M). This is reasonable considering the biology of this fungus-growing insect that lives in symbiosis with Termitomyces.…”

Section: Introductionmentioning

confidence: 99%

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Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an α‐helical conformation

Landon

Meudal

Boulanger³

et al. 2005

Biopolymers

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Stomoxyn and spinigerin belong to the class of linear cysteine-free insect antimicrobial peptides that kill a range of microorganisms, parasites, and some viruses but without any lytic activity against mammalian erythrocytes. Stomoxyn is localized in the gut epithelium of the nonvector stable fly that is sympatric with the trypanosome vector tsetse fly. Spinigerin is stored and secreted by hemocytes from the fungus-growing termite. The structure of synthetic stomoxyn and spinigerin in aqueous solution and in TFE/water mixtures was analyzed by CD and NMR spectroscopy combined with molecular modeling calculations. Stomoxyn and spinigerin adopt a flexible random coil structure in water while both assume a stable helical structure in the presence of TFE. In 50% TFE, the structure of stomoxyn is typical of cecropins, including an amphipathic helix at the N-terminus and a hydrophobic C-terminus with helical features that probably fold in a helical conformation at higher TFE concentration. In contrast to stomoxyn, spinigerin acquires very rapidly a helical conformation. In 10% TFE the helix is highly bent and the structure is poorly defined. In 50% TFE, the helical structure is well defined all along its sequence, and the slightly bent alpha-helix displays an amphiphilic character, as observed for magainin 2. The structural similarities between stomoxyn and cecropin A from Hyalophora cecropia and between spinigerin and magainin 2 suggest a similar mode of action on the bacterial membranes of both pairs of peptides. Our results also confirm that TFE induces helix formation and propagation for amino acids showing helical propensity in water but also enhances the helix propagation propensity of nonpolar beta-branched residues.

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Section: Discussionmentioning

confidence: 99%

Section: Nuclear Magnetic Resonance and Structure Calculationsmentioning

confidence: 99%

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Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an α‐helical conformation

Landon

Meudal

Boulanger³

et al. 2005

Biopolymers

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“…The balance between antimicrobial and hemolytic effects has been discussed in numerous works [116,[140][141][142][143][144][145][146][147][148][149][150][151]. The hemolytic effect is especially pronounced for Ltc 2a (Table 4).…”

Section: Hemolysismentioning

confidence: 99%

Latarcins: versatile spider venom peptides

Dubovskii

Vassilevski

Kozlov

et al. 2015

Cell. Mol. Life Sci.

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Arthropod venoms feature the presence of cytolytic peptides believed to act synergetically with neurotoxins to paralyze prey or deter aggressors. Many of them are linear, i.e., lack disulfide bonds. When isolated from the venom, or obtained by other means, these peptides exhibit common properties. They are cationic; being mostly disordered in aqueous solution, assume amphiphilic α-helical structure in contact with lipid membranes; and exhibit general cytotoxicity, including antifungal, antimicrobial, hemolytic, and anticancer activities. To suit the pharmacological needs, the activity spectrum of these peptides should be modified by rational engineering. As an example, we provide a detailed review on latarcins (Ltc), linear cytolytic peptides from Lachesana tarabaevi spider venom. Diverse experimental and computational techniques were used to investigate the spatial structure of Ltc in membrane-mimicking environments and their effects on model lipid bilayers. The antibacterial activity of Ltc was studied against a panel of Gram-negative and Gram-positive bacteria. In addition, the action of Ltc on erythrocytes and cancer cells was investigated in detail with confocal laser scanning microscopy. In the present review, we give a critical account of the progress in the research of Ltc. We explore the relationship between Ltc structure and their biological activity and derive molecular characteristics, which can be used for optimization of other linear peptides. Current applications of Ltc and prospective use of similar membrane-active peptides are outlined.

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“…gramicidins (13), pardaxin (14), mellitins (100% at 10 M) (15,16), mastorpans (90% at 25 g/ml) (17), tachyplesins II (18), prote-grin I (19), indolicidin (7), and cathelicidins (20)). Examples of relatively nontoxic peptides include mammalian defensins (21), dermaseptins (22), spinegirin (no hemolysis at 100 M) (23), and magainin (hemolysis only at the relatively high concentration of 100 g/ml) (24).…”

mentioning

confidence: 99%

Basis for Selectivity of Cationic Antimicrobial Peptides for Bacterial Versus Mammalian Membranes

Glukhov

Stark

Burrows

et al. 2005

Journal of Biological Chemistry

261

239

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Novel cationic antimicrobial peptides typified by structures such as KKKKKKAAXAAWAAXAA-NH 2 , where X ‫؍‬ Phe/Trp, and several of their analogues display high activity against a variety of bacteria but exhibit no hemolytic activity even at high dose levels in mammalian erythrocytes. To elucidate their mechanism of action and source of selectivity for bacterial membranes, phospholipid mixtures mimicking the compositions of natural bacterial membranes (containing anionic lipids) and mammalian membranes (containing zwitterionic lipids ؉ cholesterol) were challenged with the peptides. We found that peptides readily inserted into bacterial lipid mixtures, although no insertion was detected in model "mammalian" membranes. The depth of peptide insertion into model bacterial membranes was estimated by Trp fluorescence quenching using doxyl groups variably positioned along the phospholipid acyl chains. Peptide antimicrobial activity generally increased with increasing depth of peptide insertion. The overall results, in conjunction with molecular modeling, support an initial electrostatic interaction step in which bacterial membranes attract and bind peptide dimers onto the bacterial surface, followed by the "sinking" of the hydrophobic core segment to a peptide sequence-dependent depth of ϳ2.5-8 Å into the membrane, largely parallel to the membrane surface. Antimicrobial activity was likely enhanced by the fact that the peptide sequences contain AXXXA sequence motifs, which promote their dimerization, and possibly higher oligomerization, as assessed by SDS-polyacrylamide gel analysis and fluorescence resonance energy transfer experiments. The high selectivity of these peptides for nonmammalian membranes, combined with their activity toward a wide spectrum of Gram-negative and Gram-positive bacteria and yeast, while retaining water solubility, represent significant advantages of this class of peptides.

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Solution structure of termite-derived antimicrobial peptide, spinigerin, as determined in SDS micelle by NMR spectroscopy

Cited by 27 publications

References 17 publications

Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an α‐helical conformation

Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an α‐helical conformation

Latarcins: versatile spider venom peptides

Basis for Selectivity of Cationic Antimicrobial Peptides for Bacterial Versus Mammalian Membranes

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