Drugs from venom peptides
Welp. Looks like this is real. They are using venom in a LOT of medications.
Drugs from venom peptides
Medicines with APIs derived from animal venom toxins. APIs are either native purified toxins, synthetic version of native toxins, or peptide or small-molecule peptidomimetics of native toxins.
Ref: Takacs & Nathan (2014) Animal Venoms in Medicine. In: Ecyclopedia of Toxicology, 3rd ed, Vol 1. Elsevier, Academic Press, 52.
http://toxintech.com/venom_drugs.php
TOXIN TECH DIG
Zoltan Takacs is a molecular pharmacologist and inventor specialized in the functional and genomic aspects of ligand-receptor interactions. He is the co-inventor ofDesigner Toxins, a technology platform for the high-throughput screening of animal venom toxins in search of novel therapeutic leads.
Takacs' Designer Toxin libraries resulted in leads for Kv1.3 K+ channel implicated in autoimmune diseases, and a ligand for KcsA, the first K+ channel whose structure was established by X-ray crystallography yet it lacked a selective inhibitor.
Takacs holds a Ph.D. in pharmacology fromColumbia University, he completed his postdoctoral research atRockefeller University and Yale University, and was a faculty at the University of Chicago before launchingToxinTech aimed for the development of novel therapeutic leads from animal venoms.
He is a recipient of theColumbia Earth Institute Fellowship and National Geographic Society's Emerging Explorer awards. From academia to biotech, Takacs has lectured widely around the world, and has an established international network for accessing toxin samples.His research has been featured on CNN, BBC, PBS and the National Geographic Channel
http://toxintech.com/index.php#zoltan_takacs_about
Designer Toxins Intro
Designer Toxins are peptide ligands with custom biological properties that act on a wide variety of ion channels, other cell-surface receptors, and enzymatic pathways ("receptors"). Designer Toxins are produced by a proprietary technology platform which generate thousands to millions of novel combinatorial variants of evolution-tested, target-biased animal toxins and a screening platform to isolate those hits that are active on the pharmaceutical targets of interest in their native cellular milieu or in a purified form.
Designer Toxins can be employed to identify new hits or leads for drug development, to optimize known ligands (e.g., selectivity, mechanism of action, pharmacokinetics), and to validate therapeutic target selection. Public domain examples produced by Designer Toxins are high-affinity, selective ligands for Kv1.3 and KcsA K+ channels.
Today, animal venom toxins are the source of a number of major medications, including first-in-class agents, with indications for a diverse range of diseases from cardiovascular disorders to metabolic and to chronic pain. Additionally venom toxins are the source of a number of diagnostic and drug-cosmetic agents.
http://toxintech.com/index.php#designer_toxins_introduction
Improving on nature
Designer Toxins are mosaics (chimeras) of natural toxin motifs. Consequently, they exhibit novel and fine-tuned biological properties compared to the natural templates.
Evolution-tested
The biological function of animal venoms is to immobilize and kill prey or predator in seconds to minutes. Perfected by millions of years of evolution, venom toxins target a plethora of vital receptors key to neuromuscular, cardiovascular, hemostatic, and other life functions. Toxins bind to targets with high affinity and are chemically stable.
Of 150,000 venomous animal species, there is an estimated 20 million toxins.
http://toxintech.com/index.php#designer_toxins_platform
Learning From Discontinued Toxin-Based Drugs
Most cases of drugs withdrawn from the market (voluntarily or prohibited by regulatory agencies) are related to different events, ranging from safety issues, like serious side effects, to several non-safety issues, encompassing those related to the manufacturing process, regulatory or business issues, or lack of efficacy.The foreseen toxicity of some toxin-based drugs may not be completely avoided, impairing the process at different stages of drug development.Therefore, understanding the mechanisms of toxicity is of utmost importance as an attempt to prevent post-marketing withdrawals (Siramshetty et al., 2016).
A mimetic peptide isolated from Naja spp.cobra venom, ximelagatran (Exanta®, AstraZeneca), was discontinued in 2006, due tohepatotoxic potential(King, 2011). This prodrug anticoagulant agent, orally administered,had been approvedin Europe and South America for thrombin inhibition (Eriksson et al., 2003; Koh et al., 2006; Fox and Serrano, 2007; King, 2011). While Ximelagatran was mostly well tolerated in specific trial populations, a small proportion of the treated patients developed elevated liver enzyme levels, during phase II of clinical trials, which caused the FDA to reject its approval.
A phase III study of agkisacutacin (also known as hemocoagulase) in perioperative bleeding (Wei et al., 2010) was ceased due toanaphylactic reactions(Xu et al., 2016). The enzyme, which acts on fibrinogen and fibrin, is a heterodimeric serine protease from Deinagkistrodon acutus venom whose monomers A and B are comprised of 123 and 129 amino acid residues, respectively, linked by a disulfide bond (Wei et al., 2010). On the other hand, a phase IV randomized study (NCT03270735) to evaluate the efficacy and safety of hemocoagulase injection in the treatment of moderate to severe hemoptysis is recruiting patients since 2017. However, updated information regarding the evolution of this study could not be retrieved.
https://www.frontiersin.org/articles/10.3389/fphar.2020.01132/full#B107