Scorpion Peptides: Potential Use for New Drug Development

Ben-Nasr, Hmed; Serria, Hammami Turky; Mounir, Zeghal Khaled

doi:10.1155/2013/958797

Cited by 59 publications

(49 citation statements)

References 140 publications

(159 reference statements)

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“…Assumptions made by Chen et al (2012) on its mode of action indicate that the peptide on entering the viral coat dismantles the two segments (hydrophilic and hydrophobic) as the hydrophilic partform the innermost region along with the positive charge on the peptide (Chen et al 2012). It also has a significant inhibitory role in replication-competent virus HIV-1 (Gwee et al 2002;Chen et al 2012;Hmed et al 2013). To substantiate its inhibitory activity an anti-HIV assay was done by adopting a "replication-competent" HIV-1 virus; the peptide interacted with viral particles and strongly inhibited the "replicationcompetent" HIV-1 virus (Quintero-Hernándeza et al 2013).…”

Section: As Antiviralmentioning

confidence: 99%

“…This compound can also resist the growth of gram negative and gram positive bacteria and bacterial strains that have become resistant to antibiotics (Ortiz et al 2014). Another peptide mucroporin S1 too revealed potent anti-HIV activity preventing chemokine receptor CCR5 and CXCR4 activity (Hmed et al 2013). Kn2-7 was even successful when applied topically on S. aureus infection (Ortiz et al 2014…”

Section: As Antiviralmentioning

confidence: 99%

“…Scorpion neurotoxins can bind effectively for a long time because they have a three-dimensional backbone that is highly stable by the presence of three or four DBs (Hmed et al 2013). Compounds present in scorpion venom mostly target the nervous system (Podnar 2015).…”

Section: As Neurotoxinsmentioning

confidence: 99%

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Scorpion Venom–Toxins that Aid in Drug Development: A Review

Ghosh

Roy

Nandi

et al. 2018

Int J Pept Res Ther

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Scorpion venom components have multifaceted orientation against bacterial, viral, fungal infections and other neuronal disorders. They can modulate the ion channels (K + , Na + , Cl − , Ca 2+ ) of our body and this concept has been hypothesized in formulating pharmaceuticals. The triumphant achievement of these venom components as formulated anticancer agent in Phase I and Phase II clinical trials allure researchers to excavate beneficial venom components prohibiting DNA replication in malignant tumor cells. This review brings forth the achievements of Science and Technology in classifying the venom components as therapeutics and further application in drug product development.

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Section: As Antiviralmentioning

confidence: 99%

Section: As Antiviralmentioning

confidence: 99%

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Scorpion Venom–Toxins that Aid in Drug Development: A Review

Ghosh

Roy

Nandi

et al. 2018

Int J Pept Res Ther

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“…The venom of scorpions is composed of peptides that are useful in biological and medical research (2,3). Because some venom peptides affect a wide variety of physiological processes, including cell excitability, the regulation of the heartbeat, muscle contraction, neurotransmitter release, hormonal secretion, signal transduction, and cell proliferation, they have the potential to be used in drug development (4).…”

Section: Introductionmentioning

confidence: 99%

Improved System for Constructing Bacterial cDNA Libraries From the Venom Glands of Two Iranian Scorpions

Soorki

Galehdari

Jalali

et al. 2016

Jundishapur J Nat Pharm Prod

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Background: Analyzing a cell or a tissue transcriptome is the best way to understand its functions. cDNA library construction is one of the best methods to achieve this aim, and it is used to determine the structure, functions, and expression profile of a transcriptome. In the construction of a cDNA library, bacterial hosts are very adaptive. One of the most adaptive bacterial hosts is the DH5α strain of Escherichia coli. Objectives: The venom peptides of scorpions are applicable in biological and medical research as potent drugs, as they have bioactive components; therefore, their identification is very important. In this project, we set up and improved the Clontech® In-Fusion SMARTer™ Directional cDNA library construction kit in the transcriptome analysis of the venom glands of two Iranian scorpions, Odonthubuthus doriae (O. doriae) and Mesobuthus eupeus (M. eupeus).Methods: RNA extraction and cDNA synthesis and purification were conducted on the venom glands of O. doriae and M. eupeus scorpions. cDNA libraries were constructed by cloning and transforming chemically competent bacterial cells. The blue-white screen method was used to identify the transformed cells. For finding colonies that have scorpion-related inserts, a colony PCR method was designed with specific primers for two sides of the insertion site into the vector. Results: The obtained white colonies have vectors that include cDNA related to O. doriae and M. eupeus. Conclusions:The constructed cDNA libraries of O. doriae and M. eupeus glands confirmed that a framework was created for the transcriptome analysis and peptide study of the venom glands of other scorpion species.

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“…1,2 As peptides from animal venom have been approved with highly specific bioactivities, [3][4][5] they have now become significant promising sources for peptide drugs, and scorpion venom peptide, involved in this paper, is the most representative one. 6,7 Over the past years, many bioactive peptides have been purified and characterized from scorpion venom. However, they occupied only 1% amongst all the peptides from the 1500 scorpion species in the world.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of separation properties of a modified strong cation exchange material named MEX and its application in 2D-MEX × C18 system to separate peptides from scorpion venom

Chen

et al. 2015

Analyst

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Peptides from scorpion venom represent one of the most promising drug sources for drug discovery for some specific diseases. Current challenges in their separation include high complexity, high homologies and the huge range of peptides. In this paper, a modified strong cation exchange material, named MEX, was utilised for the two-dimensional separation of peptides from complex scorpion venom. The silica-based MEX column was bonded with two functional groups; benzenesulfonic acid and cyanopropyl. To better understand its separation mechanisms, seven standard peptides with different properties were employed in an evaluation study, the results of which showed that two interactions were involved in the MEX column: electrostatic interactions based on benzenesulfonic acid groups dominated the separation of peptides; weak hydrophobic interactions introduced by cyanopropyl groups increased the column's selectivity for peptides with the same charge. This characteristic allowed the MEX column to overcome some of the drawbacks of traditional strong cation exchange (SCX) columns. Furthermore, the study showed the great effects of the acetonitrile (ACN) content, the sodium perchlorate (NaClO4) concentration and the buffer pH in the mobile phase on the peptides' retention and separation selectivity on the MEX column. Subsequently, the MEX column was combined with a C18 column to establish an off-line 2D-MEX × C18 system to separate peptides from scorpion Buthus martensi Karsch (BmK) venom. Due to complementary separation mechanisms in each dimension, a high orthogonality of 47.62% was achieved. Moreover, a good loading capacity, excellent stability and repeatability were exhibited by the MEX column, which are beneficial for its use in future preparation experiments. Therefore, the MEX column could be an alternative to the traditional SCX columns for the separation of peptides from scorpion venom.

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Scorpion Peptides: Potential Use for New Drug Development

Cited by 59 publications

References 140 publications

Scorpion Venom–Toxins that Aid in Drug Development: A Review

Scorpion Venom–Toxins that Aid in Drug Development: A Review

Improved System for Constructing Bacterial cDNA Libraries From the Venom Glands of Two Iranian Scorpions

Evaluation of separation properties of a modified strong cation exchange material named MEX and its application in 2D-MEX × C18 system to separate peptides from scorpion venom

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