You know, these guys at Nutra Pharma have me intrigued, so I went a little farther on them.
They were into "venoms".........cone snail venom, gila monster venom, and cobra venom. Ok.....there are some useful applications for venom, and research into different venoms (including bee venom, as we all know) is still ongoing, but is in its infancy at this time. Nowhere could I find where it has been seriously researched for actual therapy yet, especially for MS therapy. (And as a side note, it also appears that the poor cone snails are in jeopardy, due to all the ongoing research on them. It takes a lot of snails for a little portion of product. Small numbers mean big profits, also.)
Here's what I did find, though, and it appears it's from a fairly reputable source. I'll highlight the "bottom line", as I call it.
The moral of the story being...........especially combined with the above facts that I located regarding the company itself.........is "buyer beware".
Here's the article. Note the highlighted portion at the end.
Nat Rev Drug Discov. 2003 Oct;2(10):790-802. Related Articles, Links
Therapeutic potential of venom peptides.
Lewis RJ, Garcia ML.
Institute for Molecular Bioscience, The University of Queensland, St. Lucia 4072, Australia. firstname.lastname@example.org
Nature Reviews Drug Discovery 2, 790 -802 (2003); doi:10.1038/nrd1197
Venomous animals have evolved a vast array of peptide toxins for prey capture and defence. These peptides are directed against a wide variety of pharmacological targets, making them an invaluable source of ligands for studying the properties of these targets in different experimental paradigms. A number of these peptides have been used in vivo for proof-of-concept studies, with several having undergone preclinical or clinical development for the treatment of pain, diabetes, multiple sclerosis and cardiovascular diseases. Here we survey the pharmacology of venom peptides and assess their therapeutic prospects.
Toxins have evolved in plants, animals and microbes, often as part of defensive and/or prey-capture strategies. Although non-peptide toxins are typically orally active, peptide toxins are usually found in animal venoms associated with specialized envenomation apparatus that allows their delivery into the soft tissue of animals via subcutaneous, intramuscular or intravenous routes.
Crude venoms contain a diverse array of different peptides, many of which are bioactive. Small peptides present in the venom of cone snails, a family of widely distributed marine molluscs, are highly structured mini-proteins that have evolved in 500 species of fish-, mollusc- and worm-hunting cone snails for rapid prey immobilization and defence. Their small size, relative ease of synthesis, structural stability and target specificity make them important pharmacological probes.
Venom peptides target a wide variety of membrane-bound protein channels and receptors. Of the cone snail venom peptides characterized to date, a surprising number have been found to be highly selective for a diverse range of mammalian ion channels and receptors associated with pain signalling pathways, including the nicotinic acetylcholine receptors (-conotoxins), the noradrenaline transporter (-conopeptides), sodium channels (- and O-conotoxins), calcium channels (-conotoxins), the N-methyl-D-aspartate receptor (conantokins) and the neurotensin receptor (contulakins).
It is well established that Ca2+ influx into nerve terminals through voltage-sensitive calcium channels (VSCCs) is the trigger that initiates neurotransmitter release. -Conotoxins are unique tools with which to identify and determine the physiological role of different neuronal VSCCs and might be potent analgesics for chronic pain.
Like the structurally related VSCCs, voltage-sensitive sodium channels (VSSCs) play a key role in the nervous system. A number of these VSSC subtypes are implicated in clinical states such as pain, stroke and epilepsy. Venoms have evolved to target these channels. Although sodium channel activators are typically toxic, subtypes-elective inhibitors may have considerable therapeutic potential.
Potassium channels are a large and diverse family of proteins implicated in the regulation of many cellular functions. Of the numerous potassium channel-blocking peptides that have been identified, only a small number have shown promising results in animals.
Chloride channels are also among the many membrane proteins overexpressed in different types of cancers. Chlorotoxin isolated from the scorpion Leiurus quinquestriatus binds to specific Ca2+-activated chloride channels and certain tumours and gliomas, and so might have potential in the treatment of cancer.
The first example of a successful venom-based drug is Captopril, which inhibits the angiotensin-converting enzyme, an essential enzyme for the production of angiotensin, a vasoconstrictor associated with hypertension.
As a consequence of their high selectivity, venom peptides have proved particularly useful for in vitro and in vivo proof-of-concept studies. However, for therapeutic applications, a number of issues associated with safety, pharmacokinetics and delivery need to be addressed. It remains to be determined how many of the peptides that are present in venoms can find a clinical utility.