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Latarcins: versatile spider venom peptides

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Abstract

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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Abbreviations

AMP:

Antimicrobial peptides

CBF:

Carboxyfluorescein

CD:

Circular dichroism

CL:

Cardiolipin

CSA:

Chemical shift anisotropy

CT:

Cobra venom cytotoxins (cardiotoxins)

DOPC:

Dioleoylphosphatidylcholine

DOPE:

Dioleoylphosphatidylethanolamine

DOPG:

Dioleoylphosphatidylglycerol

DPhPC:

Diphytanoylphosphatidylcholine

EC50 :

Effective concentration producing a half-maximal effect

EST:

Expressed sequence tags

GAG:

Glycosaminoglycan

iPQM:

Inverted PQM

LP:

Linear peptides

LPS:

Lipopolysaccharide

Ltc:

Latarcins

MC:

Monte Carlo method

MD:

Molecular dynamics

MHP:

Molecular hydrophobicity potential

MIC:

Minimal inhibitory concentration

PE:

Phosphatidylethanolamine

PG:

Phosphatidylglycerol

P/L:

Peptide to lipid molar ratio

PQM:

Processing quadruplet motif

PS:

Phosphatidylserine

PTG:

Peptidoglycan

RPE:

Repetitive polypeptide elements

SDS:

Sodium dodecyl sulfate

TFE:

Trifluoroethanol

TI:

Therapeutic index

n.d.:

Not determined

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Acknowledgments

This work was supported by the Russian Foundation for Basic Research (grants 13-04-02128 awarded to P.V.D. and 13-04-00825 awarded to R.G.E.), the Program “Molecular and Cellular Biology” of the Russian Academy of Sciences, the grant NSh-1924.2014.4 from the President of the Russian Federation, and grant 14-24-00118 of the Russian Science Foundation awarded to E.V.G. Access to computational facilities of the Joint Supercomputer Center of the Russian Academy of Sciences (Moscow) is appreciated. P.V.D. expresses sincere gratitude to Maria Astapova, Lidiya Baryshnikova, and Stella Yevstigneyeva for providing valuable microbiological information. We thank Lucia Kuhn-Nentwig for advice on the cupiennin classification.

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  1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya, Moscow, 117997, Russia

    Peter V. Dubovskii, Alexander A. Vassilevski, Sergey A. Kozlov, Alexey V. Feofanov, Eugene V. Grishin & Roman G. Efremov

  2. Higher School of Economics, 20 Myasnitskaya, Moscow, 101000, Russia

    Roman G. Efremov

  3. Biological Faculty, M.V. Lomonosov Moscow State University, 1 Leninskie Gory, Moscow, 119234, Russia

    Alexey V. Feofanov

  4. Moscow Institute of Physics and Technology (State University), 9 Institutskiy per., Dolgoprudny, Moscow Region, 141700, Russia

    Roman G. Efremov

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  1. Peter V. Dubovskii
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Correspondence to Peter V. Dubovskii.

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Dubovskii, P.V., Vassilevski, A.A., Kozlov, S.A. et al. Latarcins: versatile spider venom peptides. Cell. Mol. Life Sci. 72, 4501–4522 (2015). https://doi.org/10.1007/s00018-015-2016-x

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