Snake Venom Peptides: Promising Molecules with Anti-Tumor Effects

Sarray, Sameh; Luis, José; Ayeb, Mohamed El; Marrakchi, Naziha

doi:10.5772/51263

Cited by 9 publications

(8 citation statements)

References 106 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Dimeric peptides are peptides with two subunits that are linked covalently with a disulfide bond (Sarray et al, 2013) and peptide dimerization is currently being investigated as a potential way to increase the activity of certain peptide toxins (Vizzavona et al, 2009). Except for snake venoms (Osipov et al, 2008), a dimeric scaffold in peptides is quite rare in venomous animals, although it has occasionally been reported in the venoms of some scorpions (Zamudio et al, 1997), spiders (Santos et al, 1992) and marine cone snails (Loughnan et al, 2006).…”

Section: Dimeric Peptidesmentioning

confidence: 98%

Diversity of peptide toxins from stinging ant venoms

Aili

Touchard

Escoubas³

et al. 2014

Toxicon

100

151

View full text Add to dashboard Cite

Ants (Hymenoptera: Formicidae) represent a taxonomically diverse group of arthropods comprising nearly 13,000 extant species. Sixteen ant subfamilies have individuals that possess a stinger and use their venom for purposes such as a defence against predators, competitors and microbial pathogens, for predation, as well as for social communication. They exhibit a range of activities including antimicrobial, haemolytic, cytolytic, paralytic, insecticidal and pain-producing pharmacologies. While ant venoms are known to be rich in alkaloids and hydrocarbons, ant venoms rich in peptides are becoming more common, yet remain understudied. Recent advances in mass spectrometry techniques have begun to reveal the true complexity of ant venom peptide composition. In the few venoms explored thus far, most peptide toxins appear to occur as small polycationic linear toxins, with antibacterial properties and insecticidal activity. Unlike other venomous animals, a number of ant venoms also contain a range of homodimeric and heterodimeric peptides with one or two interchain disulfide bonds possessing pore-forming, allergenic and paralytic actions. However, ant venoms seem to have only a small number of monomeric disulfide-linked peptides. The present review details the structure and pharmacology of known ant venom peptide toxins and their potential as a source of novel bioinsecticides and therapeutic agents.

show abstract

Section: Dimeric Peptidesmentioning

confidence: 98%

Diversity of peptide toxins from stinging ant venoms

Aili

Touchard

Escoubas³

et al. 2014

Toxicon

100

151

View full text Add to dashboard Cite

show abstract

“…On the other hand, this diversity opens an ample scope for the use of specific inhibitors and with fewer side effects, differently from most current anticancer therapies (radiotherapy, chemotherapy) that are not specific and target both tumor and healthy cells. Thus, in recent years, new treatments tend to focus on the specific tumor microenvironment and particularly on the inhibition of tumor angiogenesis [ 144 ]. Although, disintegrins are highly effective in binding and inhibiting integrin function, which draws attention to its therapeutic potential, most clinical studies have not progressed beyond early clinical development due to the problems of instability and immunogenicity, common to peptide-based drugs.…”

Section: Introductionmentioning

confidence: 99%

Disintegrins from Snake Venoms and their Applications in Cancer Research and Therapy

Macêdo¹,

Fox

Castro³

2015

CPPS

View full text Add to dashboard Cite

Integrins regulate diverse functions in cancer pathology and in tumor cell development and contribute to important processes such as cell shape, survival, proliferation, transcription, angiogenesis, migration, and invasion. A number of snake venom proteins have the ability to interact with integrins. Among these are the disintegrins, a family of small, non-enzymatic, and cysteine-rich proteins found in the venom of numerous snake families. The venom proteins may have a potential role in terms of novel therapeutic leads for cancer treatment. Disintegrin can target specific integrins and as such it is conceivable that they could interfere in important processes involved in carcinogenesis, tumor growth, invasion and migration. Herein we present a survey of studies involving the use of snake venom disintegrins for cancer detection and treatment. The aim of this review is to highlight the relationship of integrins with cancer and to present examples as to how certain disintegrins can detect and affect biological processes related to cancer. This in turn will illustrate the great potential of these molecules for cancer research. Furthermore, we also outline several new approaches being created to address problems commonly associated with the clinical application of peptide-based drugs such as instability, immunogenicity, and availability.

show abstract

“…They have a partially conserved structure that defines the PLA2 fold [4]. Despite this similarity, sPLA2 exhibit a wide variety of pharmacological properties such as anticoagulant, platelet aggregation inhibiting [5], bactericidal [6], anti-HIV [7], antimalarial and antiparasitic [8], antitumor [9] and antiangiogenic effects [10].…”

Section: Introductionmentioning

confidence: 99%

Biochemical and monolayer characterization of Tunisian snake venom phospholipases

Baîram

Aissa

Louati

et al. 2016

International Journal of Biological Macromolecules

Self Cite

View full text Add to dashboard Cite

The present study investigated the kinetic and interfacial properties of two secreted phospholipases isolated from Tunisian vipers'venoms: Cerastes cerastes (CC-PLA2) and Macrovipera lebetina transmediterranea (MVL-PLA2). Results show that these enzymes have great different abilities to bind and hydrolyse phospholipids. Using egg-yolk emulsions as substrate at pH 8, we found that MVL-PLA2 has a specific activity of 1473U/mg at 37°C in presence of 1mM CaCl2. Furthermore the interfacial kinetic and binding data indicate that MVL-PLA2 has a preference to the zwitterionic phosphatidylcholine monolayers (PC). Conversely, CC-PLA2 was found to be able to hydrolyse preferentially negatively charged head group phospholipids (PG and PS) and exhibits a specific activity 9 times more important (13333U/mg at 60°C in presence of 3mM CaCl2). Molecular models of both CC-PLA2 and MVL-PLA2 3D structures have been built and their electrostatic potentials surfaces have been calculated. A marked anisotropy of the overall electrostatic charge distribution leads to a significantly difference in the dipole moment intensity between the two enzymes explaining the great differences in catalytic and binding properties, which seems to be governed by the electrostatic and hydrophobic forces operative at the surface of the two phospholipases.

show abstract

Snake Venom Peptides: Promising Molecules with Anti-Tumor Effects

Cited by 9 publications

References 106 publications

Diversity of peptide toxins from stinging ant venoms

Diversity of peptide toxins from stinging ant venoms

Disintegrins from Snake Venoms and their Applications in Cancer Research and Therapy

Biochemical and monolayer characterization of Tunisian snake venom phospholipases

Contact Info

Product

Resources

About