According to the scientific understanding proposed by MIT, Similia Similbus Curentur actually means, if a a particular drug substance could be proved to produce a certain group of subjective and objective symptoms when administered to a group of healthy individuals, that drug substance could be used as a therapeutic agent to cure disease conditions in any person that are expressed by similar set of subjective and objective symptoms.
This was the objective observation regarding phenomenon of curative actions of drugs made by the genius of Dr Samuel Hahneman and proved by repeated experiments, that led to the introduction of the novel therapeutic system of ‘homeopathy’ based on the fundamental principle Similia Similibus Curentur more than two centuries ago.
Due to the primitive state of scientific knowledge available at that time, it is natural that hahnemann could not provide a scientific explanation to his observations, and he was compelled by the circumstances to explain it using the philosophical concepts of ‘dynamic energy’ and ‘vital force’.
Using the modern knowledge of biochemistry, we can now understand that hahnemann was actually observing the phenomena such as ‘molecular mimicry’ and ‘competitive inhibitions’ while talking about ‘similarity’ of drug symptoms and disease symptoms.
Drug symptoms and disease symptoms appear ‘similar’ when drug substance and disease-causing substance contain some molecules having ‘similar’ conformations, so that they could bind to ‘similar’ molecular targets in the body and produce ‘similar’ molecular errors in biochemical pathways that are expressed through ‘similar’ trains of subjective and objective symptoms. Molecules having ‘similar’ conformations can compete each other in biochemical interations, which is known as ‘molecular mimicry’ according to paradigms of modern biochemistry. It is well known how molecular mimicry and molecular competitions play big role in modern understanding of molecular therapeutics.
ESSENCE OF HAHNEMANN’S CONTRIBUTION TO BIOCHEMISTRY AND MEDICAL SCIENCE IS HIS INVENTION THAT ‘SIMILARITY’ OF MOLECULES, BY WHICH THEY EXHIBIT MOLECULAR MIMICRY AND MOLECULAR COMPETITION, COULD BE IDENTIFIED BY OBSERVING THE ‘SIMILARITY’ OF SYMPTOMS THEY PRODUCE WHEN APPLIED IN LIVING BODIES!
Molecular mimicry and competitive inhibition are two phenomena that play significant roles in both the pathogenesis of diseases and the mechanism of action of many drugs.
Molecular mimicry occurs when a foreign antigen shares structural similarities with self-peptides or proteins in the host. This similarity can lead to an immune response that mistakenly targets the host’s own cells, resulting in autoimmune diseases. The immune system’s failure to distinguish between the foreign antigen and the host’s own cells can lead to the destruction of healthy tissue. A well-known example is rheumatic fever, where antibodies directed against Streptococcus bacteria cross-react with human heart tissue, leading to heart damage.
In the context of disease processes, molecular mimicry is a critical mechanism by which infections can precipitate autoimmune diseases. It highlights the importance of the immune system’s specificity and the delicate balance required to protect the body without damaging it.
Molecular mimicry plays a crucial role in both pathology and therapeutics, underlying many autoimmune diseases and offering innovative approaches to treatment. Below are additional examples that further illustrate the concept of molecular mimicry in these contexts.
Guillain-Barré Syndrome is an autoimmune disorder that affects the peripheral nervous system, often triggered by an infection. The classic example is the relationship between GBS and infections caused by Campylobacter jejuni. The outer surface proteins of this bacterium resemble components of the myelin sheath of peripheral nerves. The immune response directed against the bacterium can mistakenly target and damage the myelin sheath, leading to muscle weakness and paralysis.
In Type 1 Diabetes, molecular mimicry may play a role where viral proteins from agents such as Coxsackie B virus share structural similarities with beta-cell antigens in the pancreas. The immune system’s attack on the virus can inadvertently destroy beta cells, leading to insulin deficiency and diabetes.
Multiple Sclerosis is a chronic autoimmune disease where the immune system attacks the myelin sheath of nerve fibers in the brain and spinal cord. There is evidence to suggest that viral or bacterial antigens may mimic myelin or other neural proteins, triggering an immune response that mistakenly damages the central nervous system.
In autoimmune diseases, therapeutic peptides designed to mimic self-antigens can be introduced to induce tolerance in the immune system. This approach aims to train the immune system not to attack the body’s own tissues. For instance, in MS, researchers are exploring peptides that mimic myelin basic protein (MBP) to teach the immune system to recognize it as harmless, potentially reducing the autoimmune attack on the myelin sheath.
Monoclonal antibodies that mimic natural immune system molecules can block or modulate immune system activity. For example, in rheumatoid arthritis, mAbs may be designed to mimic antigens that bind to and neutralize pro-inflammatory cytokines, such as tumor necrosis factor (TNF), thereby reducing inflammation and joint damage.
Vaccines exploit molecular mimicry by introducing an antigen that mimics a pathogen component into the body, without causing disease. This stimulates the immune system to produce a response, including memory cells that will recognize and fight the actual pathogen if encountered in the future. For therapeutic vaccines against cancer, researchers are developing vaccines that introduce tumor antigens to the immune system, aiming to trigger a response that targets and destroys cancer cells.
Competitive inhibition, on the other hand, is a biochemical process where a molecule similar in structure to the substrate of an enzyme competes with the substrate for binding to the enzyme’s active site. This mechanism is relevant in both the physiology of living organisms and the pharmacology of drugs. In the body, competitive inhibition can regulate metabolic pathways, ensuring that they do not proceed too quickly or too slowly, maintaining metabolic balance.
Molecular competition, a fundamental concept in biochemistry and pharmacology, involves molecules competing for binding sites on enzymes, receptors, or other targets. This principle is pivotal in understanding drug action, resistance, and the emergence of certain diseases. Below are more examples illustrating molecular competition in both pathology and therapeutics.
In pharmacology, competitive inhibition is a principle used in the design of many drugs, particularly those used to treat diseases by inhibiting enzymes. For example, statins, which are used to lower cholesterol levels, work by competitively inhibiting HMG-CoA reductase, a key enzyme in cholesterol synthesis. Similarly, many antibiotics act by competitively inhibiting enzymes essential for bacterial survival, thereby killing or inhibiting the growth of the bacteria.
In the realm of pharmacology and toxicology, competitive relationships between drugs or between a toxin and an antidote play a crucial role in therapeutic interventions. Such relationships are exemplified by the actions of methotrexate, sulfa drugs, and the use of ethanol in methanol poisoning. These examples highlight how competitive inhibition can be leveraged for therapeutic benefits, either by directly competing for enzyme binding sites or by influencing metabolic pathways.
Methotrexate serves as a competitive inhibitor for the enzyme dihydrofolate reductase (DHFR). By mimicking the structure of dihydrofolate, methotrexate binds to DHFR with a higher affinity than its natural substrate, effectively blocking the enzyme’s activity. This inhibition leads to a decrease in tetrahydrofolate synthesis, a cofactor necessary for the synthesis of purines and pyrimidines, and thus, inhibits DNA and RNA synthesis. This mechanism is particularly effective against rapidly dividing cells, such as cancer cells in leukemia and tumors, as well as in the suppression of immune cell proliferation in autoimmune diseases like rheumatoid arthritis.
Sulfa drugs, or sulfonamides, are another classic example of competitive inhibition at work. These antibiotics bear a structural similarity to para-aminobenzoic acid (PABA), a substrate necessary for bacterial folate synthesis. By competing with PABA for the active site of the enzyme dihydropteroate synthase, sulfa drugs prevent the synthesis of dihydrofolate, thereby inhibiting bacterial growth. This competitive inhibition is crucial for the effectiveness of sulfa drugs in treating bacterial infections.
The treatment of methanol poisoning with ethanol is a fascinating application of competitive inhibition in toxicology. Methanol itself is only mildly toxic, but its metabolites, formaldehyde and formic acid, cause the severe effects associated with poisoning, including metabolic acidosis, visual disturbances, and potential blindness. Ethanol competes with methanol for the enzyme alcohol dehydrogenase (ADH), which is responsible for the metabolism of both alcohols. By administering ethanol, which has a higher affinity for ADH, the metabolism of methanol is slowed, decreasing the formation of toxic metabolites and allowing methanol to be excreted from the body unchanged. This competitive relationship is exploited therapeutically to manage methanol poisoning and prevent its severe consequences.
These examples illustrate the fundamental principle of competitive inhibition and its application in various therapeutic contexts. By understanding and exploiting the competitive relationships between molecules, medical science can effectively treat a range of conditions, from infections and poisonings to cancer and autoimmune diseases. This principle underscores the importance of molecular mimicry in drug design and therapeutic strategies, offering a powerful tool against disease and toxicity.
In bacteria, the overuse of antibiotics has led to the emergence of resistance mechanisms, many of which involve molecular competition. For example, some bacteria produce beta-lactamase enzymes that compete with the antibiotic molecules for the active site of penicillin-binding proteins (PBPs), which are essential for bacterial cell wall synthesis. By binding to and inactivating the antibiotics, these enzymes protect the bacteria, allowing them to survive and multiply despite antibiotic treatment.
Certain viruses, including HIV, use molecular competition to gain entry into host cells. HIV’s surface glycoprotein gp120 binds to the CD4 receptor on the surface of T cells. This interaction is competitive, as other molecules, including some immune factors, can also bind to CD4, potentially blocking viral entry. Therapies that mimic the CD4 binding site can competitively inhibit HIV from attaching to and entering cells.
Angiotensin-converting enzyme (ACE) inhibitors are a class of drugs used to treat hypertension and heart failure. They work by competitively inhibiting the enzyme ACE, which is involved in the renin-angiotensin system (RAS) that regulates blood pressure. By blocking ACE, these drugs prevent the conversion of angiotensin I to angiotensin II, a potent vasoconstrictor, thereby lowering blood pressure.
In the treatment of hormone-sensitive breast cancer, aromatase inhibitors play a crucial role. These drugs competitively inhibit the enzyme aromatase, which is involved in the synthesis of estrogen. By reducing estrogen levels, aromatase inhibitors can slow or stop the growth of hormone-receptor-positive breast cancer cells, which rely on estrogen to proliferate.
In cases of poisoning with substances such as organophosphates (found in some pesticides and nerve agents), drugs like pralidoxime can act as antidotes through molecular competition. Organophosphates inhibit the enzyme acetylcholinesterase, leading to an accumulation of acetylcholine and continuous stimulation of muscles and glands. Pralidoxime competes with the organophosphate for binding to acetylcholinesterase, reactivating the enzyme and alleviating symptoms of poisoning.
These examples underscore the importance of molecular competition in both the development of diseases and the creation of therapeutic strategies. By understanding and leveraging the competitive interactions between molecules, researchers and clinicians can devise more effective treatments for a wide array of conditions.
Both phenomena of molecular mimicry and molecular competition highlight the complexity of biological systems and the intricate balance that governs bodily functions and responses. Understanding molecular mimicry and competitive inhibition is crucial for developing therapeutic strategies that can effectively treat diseases without harming the body. It underscores the importance of targeted drug design and the need for a deep understanding of the molecular mechanisms underlying diseases and drug actions.
Actually, the phenomena of ‘molecular mimicry’ and ‘molecular competitions’ and their role in therapeutics were first observed by Hahnemann, and developed into the therapeutic principle of Similia Similibus Curentur, which modern scientific community is still hesitating to understand or recognize!
REDEFINING HOMEOPATHY 