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Toxins
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Venom and Toxin as Targeted Therapy
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Venom and Toxin as Targeted Therapy

A special issue of Toxins (ISSN 2072-6651).

Deadline for manuscript submissions: closed (28 February 2019) | Viewed by 83798

Printed Edition Available!
A printed edition of this Special Issue is available here.

Special Issue Editor

Prof. Dr. Hang Fai (Henry) Kwok

E-Mail Website
Guest Editor
Faculty of Health Sciences (E12), University of Macau, Avenida de Universidade, Macau, China
Interests: protease biochemistry; toxins; anti-cancer drug discovery; antibody therapy; venom-based peptides; prognostic and diagnostic biomarkers; proteomics
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Targeted therapy describes taking specific medications for treatment of particular diseases, such as cancer, diabetes, heart disease, etc. One of the most exciting recent developments in targeted therapies is the isolation of disease-specific molecules from natural resources, such as animal venoms and plant metabolites/toxins, to use as templates to design new drugs. As venom proteins/peptides and toxins naturally target mammalian receptors, they show high specificity and selectivity towards defined cell membrane ion channels and receptors. 

The focus of this Special Issue of Toxins will be on the most recent advances related to the animal venom/plant toxin as medicinal therapy. Recent advances in venom/toxin targeted cancer therapy and immunotherapy will be addressed. The discussion on using novel disease-specific venom-based protein/peptide/toxin along with currently available FDA approved drugs as combinatorial treatment will also be encouraged in this context. Finally, an overview of some selected promising venom-based peptides/toxins potentially able to address the forthcoming challenges in this field will be included. Both research (in particular) and review articles proposing novelties or overviews, respectively, are welcome.

Prof. Dr. Hang Fai (Henry) Kwok
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Venom peptides
  • Toxins
  • Targeted therapy
  • Immunotherapy
  • Combinatorial treatment
  • Cancer
  • Diabetes
  • Heart disease

Published Papers (15 papers)

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Editorial

Jump to: Research, Review

2 pages, 193 KiB  
Editorial
Venom Toxins as Potential Targeted Therapies
by Hang Fai Kwok
Toxins 2019, 11(6), 338; https://doi.org/10.3390/toxins11060338 - 13 Jun 2019
Cited by 1 | Viewed by 1980
Abstract
Targeted therapy has been a very hot research topic in the last decade [...] Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)

Research

Jump to: Editorial, Review

12 pages, 2782 KiB  
Article
Bee Venom Alleviates Atopic Dermatitis Symptoms through the Upregulation of Decay-Accelerating Factor (DAF/CD55)
by Yenny Kim, Youn-Woo Lee, Hangeun Kim and Dae Kyun Chung
Toxins 2019, 11(5), 239; https://doi.org/10.3390/toxins11050239 - 26 Apr 2019
Cited by 14 | Viewed by 3995
Abstract
Bee venom (BV)—a complex mixture of peptides and toxic proteins including phospholipase A2 and melittin—promotes blood clotting. In this study, we investigated the anti-atopic properties of BV and the mechanism associated with its regulation of the complement system. BV treatment upregulated the mRNA [...] Read more.
Bee venom (BV)—a complex mixture of peptides and toxic proteins including phospholipase A2 and melittin—promotes blood clotting. In this study, we investigated the anti-atopic properties of BV and the mechanism associated with its regulation of the complement system. BV treatment upregulated the mRNA and protein levels of CD55 in THP-1 cells. Further experiments revealed that the phosphorylation of ERK was associated with upregulation of CD55. A complement-dependent cytotoxicity assay and a bacteria-killing assay showed that BV inactivated the complement system through the induction of CD55. The serum levels of C3 convertase (C3C) and Membrane attack complex (MAC) increased, while CD55 decreased in mice with AD-like lesions from DNCB treatment. However, the levels were inverted when the AD-like mice were treated with BV using subcutaneous injection, and we observed that the AD symptoms were alleviated. BV is often used to treat AD but its mechanism has not been elucidated. Here, we suggest that BV alleviates AD through the inactivation of the complement system, especially by the induction of CD55. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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12 pages, 3096 KiB  
Article
A Hylarana latouchii Skin Secretion-Derived Novel Bombesin-Related Pentadecapeptide (Ranatensin-HLa) Evoke Myotropic Effects on the in vitro Rat Smooth Muscles
by Yan Lin, Nan Hu, Haoyang He, Chengbang Ma, Mei Zhou, Lei Wang and Tianbao Chen
Toxins 2019, 11(4), 204; https://doi.org/10.3390/toxins11040204 - 05 Apr 2019
Cited by 4 | Viewed by 3010
Abstract
Amphibians have developed successful defensive strategies for combating predators and invasive microorganisms encountered in their broad range of environments, which involve secretion of complex cocktails of noxious, toxic and diverse bioactive molecules from the skins. In recent years, amphibian skin secretions have been [...] Read more.
Amphibians have developed successful defensive strategies for combating predators and invasive microorganisms encountered in their broad range of environments, which involve secretion of complex cocktails of noxious, toxic and diverse bioactive molecules from the skins. In recent years, amphibian skin secretions have been considered as an extraordinary warehouse for the discovery of therapeutic medicines. In this study, through bioactivity screening of the Hylarana latouchii skin secretion-derived fractions, a novel peptide belonging to ranatensin subfamily (ranatensin-HLa) was discovered, and structurally and pharmacologically-characterised. It consists of 15 amino acid residues, pGlu-NGDRAPQWAVGHFM-NH2, and its synthetic replicate was found to exhibit pharmacological activities on increasing the contraction of the in vitro rat bladder and uterus smooth muscles. Corresponding characteristic sigmoidal dose-response curves with EC50 values of 7.1 nM and 5.5 nM were produced, respectively, in bladder and uterus. Moreover, the precursor of ranatensin-HLa showed a high degree of similarity to those of bombesin-like peptides from Odorrana grahami and Odorrana schmackeri. Hylarana latouchii skin continues to serve as a storehouse with diverse lead compounds for the development of therapeutically effective medicines. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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13 pages, 2169 KiB  
Article
First Characterization of The Venom from Apis mellifera syriaca, A Honeybee from The Middle East Region
by Jacinthe Frangieh, Yahya Salma, Katia Haddad, Cesar Mattei, Christian Legros, Ziad Fajloun and Dany El Obeid
Toxins 2019, 11(4), 191; https://doi.org/10.3390/toxins11040191 - 30 Mar 2019
Cited by 40 | Viewed by 6872
Abstract
Bee venom is a mixture of several components with proven therapeutic benefits, among which are anti-inflammatory, analgesic, and various cardiovascular conditions. In this work, we analyzed for the first time the proteomic content and biological properties of the crude venom from Apis mellifera [...] Read more.
Bee venom is a mixture of several components with proven therapeutic benefits, among which are anti-inflammatory, analgesic, and various cardiovascular conditions. In this work, we analyzed for the first time the proteomic content and biological properties of the crude venom from Apis mellifera syriaca, a honeybee from the Middle East region. Using high-performance liquid chromatography-tandem mass spectrometry, we evidence the venom contains phospholipase A2, hyaluronidase, mast cell-degranulating peptide, adolapin, apamin, and melittin. The latter was purified by solid phase extraction method (SPE) and tested in parallel with crude venom for biological activities. Precisely, crude venom—but not melittin—exhibited antibacterial activity against Staphylococcus aureus and Pseudomonas aeruginosa strains. Alongside, hemolytic activity was observed in human blood subjected to the venom at high doses. A. mellifera syriaca venom displayed antioxidant activities, and not surprisingly, PLA2 catalytic activity. Eventually, the venom proved to exert antiproliferative effects against MCF-7 and 3T3 cancer cells lines. This first report of a new bee venom opens new avenues for therapeutic uses of bee venoms. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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15 pages, 1745 KiB  
Article
Pharmacokinetic Properties of the Nephrotoxin Orellanine in Rats
by Deman Najar, Börje Haraldsson, Annika Thorsell, Carina Sihlbom, Jenny Nyström and Kerstin Ebefors
Toxins 2018, 10(8), 333; https://doi.org/10.3390/toxins10080333 - 17 Aug 2018
Cited by 6 | Viewed by 6777
Abstract
Orellanine is a nephrotoxin found in mushrooms of the Cortinarius family. Accidental intake of this substance may cause renal failure. Orellanine is specific for proximal tubular cells and could, therefore, potentially be used as treatment for metastatic renal cancer, which originates from these [...] Read more.
Orellanine is a nephrotoxin found in mushrooms of the Cortinarius family. Accidental intake of this substance may cause renal failure. Orellanine is specific for proximal tubular cells and could, therefore, potentially be used as treatment for metastatic renal cancer, which originates from these cells. However, more information is needed about the distribution and elimination of orellanine from the body to understand its potential use for therapy. In this study, 5 mg/kg orellanine (unlabeled and 3H-labeled) was injected intravenously in rats (Wistar and Sprague Dawley). Distribution was measured (Wistar rats, n = 10, n = 12) using radioluminography and the highest amount of orellanine was found in the kidney cortex and bladder at all time-points investigated. The pharmacokinetic properties of orellanine was investigated using LC-MS/MS and β-scintillation to measure the amount of orellanine in plasma. Three groups of rats were investigated: control rats with intact kidneys (n = 10) and two groups with bilateral renal artery ligation (n = 7) where animals in one of these groups were treated with peritoneal dialysis (n = 8). Using LC-MS/MS, the half-life of orellanine was found to be 109 ± 6 min in the controls. In the groups with ligated renal arteries, orellanine had a half-life of 756 ± 98 min without and 238 ± 28 min with dialysis. Thus, orellanine was almost exclusively eliminated by glomerular filtration as well as by peritoneal dialysis. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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11 pages, 1522 KiB  
Article
Biological Activities of Cationicity-Enhanced and Hydrophobicity-Optimized Analogues of an Antimicrobial Peptide, Dermaseptin-PS3, from the Skin Secretion of Phyllomedusa sauvagii
by Yining Tan, Xiaoling Chen, Chengbang Ma, Xinping Xi, Lei Wang, Mei Zhou, James F. Burrows, Hang Fai Kwok and Tianbao Chen
Toxins 2018, 10(8), 320; https://doi.org/10.3390/toxins10080320 - 07 Aug 2018
Cited by 18 | Viewed by 4002
Abstract
The skin secretions of the subfamily Phyllomedusinae have long been known to contain a number of compounds with antimicrobial potential. Herein, a biosynthetic dermaseptin-precursor cDNA was obtained from a Phyllomedusa sauvagii skin secretion-derived cDNA library, and thereafter, the presence of the mature peptide, [...] Read more.
The skin secretions of the subfamily Phyllomedusinae have long been known to contain a number of compounds with antimicrobial potential. Herein, a biosynthetic dermaseptin-precursor cDNA was obtained from a Phyllomedusa sauvagii skin secretion-derived cDNA library, and thereafter, the presence of the mature peptide, namely dermaseptin-PS3 (DPS3), was confirmed by LC–MS/MS. Moreover, this naturally occurring peptide was utilized to design two analogues, K5, 17-DPS3 (introducing two lysine residues at positions 5 and 17 to replace acidic amino acids) and L10, 11-DPS3 (replacing two neutral amino acids with the hydrophobic amino acid, leucine), improving its cationicity on the polar/unipolar face and hydrophobicity in a highly conserved sequence motif, respectively. The results in regard to the two analogues show that either increasing cationicity, or hydrophobicity, enhance the antimicrobial activity. Also, the latter analogue had an enhanced anticancer activity, with pretreatment of H157 cells with 1 µM L10, 11-DPS3 decreasing viability by approximately 78%, even though this concentration of peptide exhibited no haemolytic effect. However, it must be noted that in comparison to the initial peptide, both analogues demonstrate higher membrane-rupturing capacity towards mammalian red blood cells. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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13 pages, 2762 KiB  
Article
Burkholderia Lethal Factor 1, a Novel Anti-Cancer Toxin, Demonstrates Selective Cytotoxicity in MYCN-Amplified Neuroblastoma Cells
by Aleksander Rust, Sajid Shah, Guillaume M. Hautbergue and Bazbek Davletov
Toxins 2018, 10(7), 261; https://doi.org/10.3390/toxins10070261 - 27 Jun 2018
Cited by 10 | Viewed by 4234
Abstract
Immunotoxins are being investigated as anti-cancer therapies and consist of a cytotoxic enzyme fused to a cancer targeting antibody. All currently used toxins function via the inhibition of protein synthesis, making them highly potent in both healthy and transformed cells. This non-specific cell [...] Read more.
Immunotoxins are being investigated as anti-cancer therapies and consist of a cytotoxic enzyme fused to a cancer targeting antibody. All currently used toxins function via the inhibition of protein synthesis, making them highly potent in both healthy and transformed cells. This non-specific cell killing mechanism causes dose-limiting side effects that can severely limit the potential of immunotoxin therapy. In this study, the recently characterised bacterial toxin Burkholderia lethal factor 1 (BLF1) is investigated as a possible alternative payload for targeted toxin therapy in the treatment of neuroblastoma. BLF1 inhibits translation initiation by inactivation of eukaryotic initiation translation factor 4A (eIF4A), a putative anti-cancer target that has been shown to regulate a number of oncogenic proteins at the translational level. We show that cellular delivery of BLF1 selectively induces apoptosis in neuroblastoma cells that display MYCN amplification but has little effect on non-transformed cells. Future immunotoxins based on this enzyme may therefore have higher specificity towards MYCN-amplified cancer cells than more conventional ribosome-inactivating proteins, leading to an increased therapeutic window and decreased side effects. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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12 pages, 1557 KiB  
Article
Domain II of Pseudomonas Exotoxin Is Critical for Efficacy of Bolus Doses in a Xenograft Model of Acute Lymphoblastic Leukemia
by Fabian Müller, Tyler Cunningham, Richard Beers, Tapan K. Bera, Alan S. Wayne and Ira Pastan
Toxins 2018, 10(5), 210; https://doi.org/10.3390/toxins10050210 - 21 May 2018
Cited by 8 | Viewed by 3838
Abstract
Moxetumomab pasudotox is a fusion protein of a CD22-targeting antibody and Pseudomonas exotoxin. Minutes of exposure to Moxetumomab achieves similar cell killing than hours of exposure to a novel deimmunized variant against some acute lymphoblastic leukemia (ALL). Because blood levels fall quickly, Moxetumomab [...] Read more.
Moxetumomab pasudotox is a fusion protein of a CD22-targeting antibody and Pseudomonas exotoxin. Minutes of exposure to Moxetumomab achieves similar cell killing than hours of exposure to a novel deimmunized variant against some acute lymphoblastic leukemia (ALL). Because blood levels fall quickly, Moxetumomab is more than 1000-fold more active than the deimmunized variant in vivo. We aimed to identify which part of Moxetumomab increases in vivo efficacy and generated five immunotoxins, tested time-dependent activity, and determined the efficacy in a KOPN-8 xenograft model. Full domain II shortened the time cells had to be exposed to die to only a few minutes for some ALL; deimmunized domain III consistently extended the time. Against KOPN-8, full domain II accelerated time to arrest protein synthesis by three-fold and tripled PARP-cleavage. In vivo efficacy was increased by more than 10-fold by domain II and increasing size, and therefore half-life enhanced efficacy two- to four-fold. In summary, in vivo efficacy is determined by the time cells have to be exposed to immunotoxin to die and serum half-life. Thus, domain II is most critical for activity against some ALL treated with bolus doses; however, immunotoxins lacking all but the furin-cleavage site of domain II may be advantageous when treating continuously. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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10 pages, 2868 KiB  
Article
Bee Venom Phospholipase A2 Alleviate House Dust Mite-Induced Atopic Dermatitis-Like Skin Lesions by the CD206 Mannose Receptor
by Dasom Shin, Won Choi and Hyunsu Bae
Toxins 2018, 10(4), 146; https://doi.org/10.3390/toxins10040146 - 02 Apr 2018
Cited by 14 | Viewed by 5467
Abstract
Atopic dermatitis (AD) is a chronic inflammatory skin disease characterized by highly pruritic, erythematous, and eczematous skin plaques. We previously reported that phospholipase A2 (PLA2) derived from bee venom alleviates AD-like skin lesions induced by 2,4-dinitrochlorobenzene (DNCB) and house dust mite extract ( [...] Read more.
Atopic dermatitis (AD) is a chronic inflammatory skin disease characterized by highly pruritic, erythematous, and eczematous skin plaques. We previously reported that phospholipase A2 (PLA2) derived from bee venom alleviates AD-like skin lesions induced by 2,4-dinitrochlorobenzene (DNCB) and house dust mite extract (Dermatophagoides farinae extract, DFE) in a murine model. However, the underlying mechanisms of PLA2 action in actopic dermatitis remain unclear. In this study, we showed that PLA2 treatment inhibited epidermal thickness, serum immunoglobulin E (IgE) and cytokine levels, macrophage and mast cell infiltration in the ear of an AD model induced by DFE and DNCB. In contrast, these effects were abrogated in CD206 mannose receptor-deficient mice exposed to DFE and DNCB in the ear. These data suggest that bvPLA2 alleviates atopic skin inflammation via interaction with CD206. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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4064 KiB  
Article
Anti-Helicobacter pylori Properties of the Ant-Venom Peptide Bicarinalin
by Jesus Guzman, Nathan Téné, Axel Touchard, Denis Castillo, Haouaria Belkhelfa, Laila Haddioui-Hbabi, Michel Treilhou and Michel Sauvain
Toxins 2018, 10(1), 21; https://doi.org/10.3390/toxins10010021 - 29 Dec 2017
Cited by 23 | Viewed by 7213
Abstract
The venom peptide bicarinalin, previously isolated from the ant Tetramorium bicarinatum, is an antimicrobial agent with a broad spectrum of activity. In this study, we investigate the potential of bicarinalin as a novel agent against Helicobacter pylori, which causes several gastric [...] Read more.
The venom peptide bicarinalin, previously isolated from the ant Tetramorium bicarinatum, is an antimicrobial agent with a broad spectrum of activity. In this study, we investigate the potential of bicarinalin as a novel agent against Helicobacter pylori, which causes several gastric diseases. First, the effects of synthetic bicarinalin have been tested against Helicobacter pylori: one ATCC strain, and forty-four isolated from stomach ulcer biopsies of Peruvian patients. Then the cytoxicity of bicarinalin on human gastric cells and murine peritoneal macrophages was measured using XTT and MTT assays, respectively. Finally, the preventive effect of bicarinalin was evaluated by scanning electron microscopy using an adherence assay of H. pylori on human gastric cells treated with bicarinalin. This peptide has a potent antibacterial activity at the same magnitude as four antibiotics currently used in therapies against H. pylori. Bicarinalin also inhibited adherence of H. pylori to gastric cells with an IC50 of 0.12 μg·mL−1 and had low toxicity for human cells. Scanning electron microscopy confirmed that bicarinalin can significantly decrease the density of H. pylori on gastric cells. We conclude that Bicarinalin is a promising compound for the development of a novel and effective anti-H. pylori agent for both curative and preventive use. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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3534 KiB  
Article
Alternagin-C (ALT-C), a Disintegrin-Like Cys-Rich Protein Isolated from the Venom of the Snake Rhinocerophis alternatus, Stimulates Angiogenesis and Antioxidant Defenses in the Liver of Freshwater Fish, Hoplias malabaricus
by Diana Amaral Monteiro, Heloisa Sobreiro Selistre-de-Araújo, Driele Tavares, Marisa Narciso Fernandes, Ana Lúcia Kalinin and Francisco Tadeu Rantin
Toxins 2017, 9(10), 307; https://doi.org/10.3390/toxins9100307 - 28 Sep 2017
Cited by 4 | Viewed by 4766
Abstract
Alternagin-C (ALT-C) is a disintegrin-like protein isolated from Rhinocerophis alternatus snake venom, which induces endothelial cell proliferation and angiogenesis. The aim of this study was to evaluate the systemic effects of a single dose of alternagin-C (0.5 mg·kg−1, via intra-arterial) on [...] Read more.
Alternagin-C (ALT-C) is a disintegrin-like protein isolated from Rhinocerophis alternatus snake venom, which induces endothelial cell proliferation and angiogenesis. The aim of this study was to evaluate the systemic effects of a single dose of alternagin-C (0.5 mg·kg−1, via intra-arterial) on oxidative stress biomarkers, histological alterations, vascular endothelial growth factor (VEGF) production, and the degree of vascularization in the liver of the freshwater fish traíra, Hoplias malabaricus, seven days after the initiation of therapy. ALT-C treatment increased VEGF levels and hepatic angiogenesis. ALT-C also enhanced hepatic antioxidant enzymes activities such as superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase, decreasing the basal oxidative damage to lipids and proteins in the fish liver. These results indicate that ALT-C improved hepatic tissue and may play a crucial role in tissue regeneration mechanisms. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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Review

Jump to: Editorial, Research

12 pages, 597 KiB  
Review
Malaysian Cobra Venom: A Potential Source of Anti-Cancer Therapeutic Agents
by Syafiq Asnawi Zainal Abidin, Yee Qian Lee, Iekhsan Othman and Rakesh Naidu
Toxins 2019, 11(2), 75; https://doi.org/10.3390/toxins11020075 - 01 Feb 2019
Cited by 16 | Viewed by 7115
Abstract
Cancer is a deadly disease and there is an urgent need for the development of effective and safe therapeutic agents to treat it. Snake venom is a complex mixture of bioactive proteins that represents an attractive source of novel and naturally-derived anticancer agents. [...] Read more.
Cancer is a deadly disease and there is an urgent need for the development of effective and safe therapeutic agents to treat it. Snake venom is a complex mixture of bioactive proteins that represents an attractive source of novel and naturally-derived anticancer agents. Malaysia is one of the world’s most biodiverse countries and is home to various venomous snake species, including cobras. Naja kaouthia, Naja sumatrana, and Ophiophagus hannah are three of the most common cobra species in Malaysia and are of medical importance. Over the past decades, snake venom has been identified as a potential source of therapeutic agents, including anti-cancer agents. This present review highlights the potential anticancer activity of the venom and purified venom protein of N. kaouthia, N. sumatrana, and O. hannah. In conclusion, this review highlights the important role of the venom from Malaysian cobras as an important resource that researchers can exploit to further investigate its potential in cancer treatment. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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8 pages, 481 KiB  
Review
Snake Venoms in Cancer Therapy: Past, Present and Future
by Li Li, Jianzhong Huang and Yao Lin
Toxins 2018, 10(9), 346; https://doi.org/10.3390/toxins10090346 - 29 Aug 2018
Cited by 56 | Viewed by 11508
Abstract
Cancer is one of the leading causes of morbidity and mortality worldwide, and the discovery of new drugs for cancer therapy is one of the most important objectives for the pharmaceutical industry. Snake venoms are complex mixtures containing different peptides, proteins, enzymes, carbohydrates [...] Read more.
Cancer is one of the leading causes of morbidity and mortality worldwide, and the discovery of new drugs for cancer therapy is one of the most important objectives for the pharmaceutical industry. Snake venoms are complex mixtures containing different peptides, proteins, enzymes, carbohydrates and other bioactive molecules, which are secreted by the snake in the predation or defending against threats. Understanding the snake venoms may turn the toxins into a valuable source of new lead compounds in drug discovery. Captopril, the first angiotensin-converting enzyme inhibitor approved in 1981 by FDA, was designed based on the structure of a peptide isolated from the snake venom. The earliest reports about snake venoms used in cancer treatments appeared in the 1930s. Since then, numerous studies on the activities, isolations, purifications and structure elucidations of the components from snake venoms were published. The comprehensive structural and functional investigations of snake venoms would contribute to the development of novel anti-cancer drugs. Our review will focus on the past, present and the future of the studies on snake venoms in cancer target therapy. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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14 pages, 920 KiB  
Review
The Development of Toad Toxins as Potential Therapeutic Agents
by Ji Qi, Abu Hasanat Md Zulfiker, Chun Li, David Good and Ming Q. Wei
Toxins 2018, 10(8), 336; https://doi.org/10.3390/toxins10080336 - 20 Aug 2018
Cited by 49 | Viewed by 7431
Abstract
Toxins from toads have long been known to contain rich chemicals with great pharmaceutical potential. Recent studies have shown more than 100 such chemical components, including peptides, steroids, indole alkaloids, bufogargarizanines, organic acids, and others, in the parotoid and skins gland secretions from [...] Read more.
Toxins from toads have long been known to contain rich chemicals with great pharmaceutical potential. Recent studies have shown more than 100 such chemical components, including peptides, steroids, indole alkaloids, bufogargarizanines, organic acids, and others, in the parotoid and skins gland secretions from different species of toads. In traditional Chinese medicine (TCM), processed toad toxins have been used for treating various diseases for hundreds of years. Modern studies, including both experimental and clinical trials, have also revealed the molecular mechanisms that support the development of these components into medicines for the treatment of inflammatory diseases and cancers. More recently, there have been studies that demonstrated the therapeutic potential of toxins from other species of toads, such as Australian cane toads. Previous reviews mostly focused on the pharmaceutical effects of the whole extracts from parotoid glands or skins of toads. However, to fully understand the molecular basis of toad toxins in their use for therapy, a comprehensive understanding of the individual compound contained in toad toxins is necessary; thus, this paper seeks to review the recent studies of some typical compounds frequently identified in toad secretions. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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10 pages, 942 KiB  
Review
Bouganin, an Attractive Weapon for Immunotoxins
by Massimo Bortolotti, Andrea Bolognesi and Letizia Polito
Toxins 2018, 10(8), 323; https://doi.org/10.3390/toxins10080323 - 08 Aug 2018
Cited by 13 | Viewed by 4048
Abstract
Bougainvillea (Bougainvillea spectabilis Willd.) is a plant widely used in folk medicine and many extracts from different tissues of this plant have been employed against several pathologies. The observation that leaf extracts of Bougainvillea possess antiviral properties led to the purification and [...] Read more.
Bougainvillea (Bougainvillea spectabilis Willd.) is a plant widely used in folk medicine and many extracts from different tissues of this plant have been employed against several pathologies. The observation that leaf extracts of Bougainvillea possess antiviral properties led to the purification and characterization of a protein, named bouganin, which exhibits typical characteristics of type 1 ribosome-inactivating proteins (RIPs). Beyond that, bouganin has some peculiarities, such as a higher activity on DNA with respect to ribosomal RNA, low systemic toxicity, and immunological properties quite different than other RIPs. The sequencing of bouganin and the knowledge of its three-dimensional structure allowed to obtain a not immunogenic mutant of bouganin. These features make bouganin a very attractive tool as a component of immunotoxins (ITs), chimeric proteins obtained by linking a toxin to a carrier molecule. Bouganin-containing ITs showed very promising results in the experimental treatment of both hematological and solid tumors, and one bouganin-containing IT has entered Phase I clinical trial. In this review, we summarize the milestones of the research on bouganin such as bouganin chemico-physical characteristics, the structural properties and de-immunization studies. In addition, the in vitro and in vivo results obtained with bouganin-containing ITs are summarized. Full article
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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