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CHEMISTRY IN EVERYDAY LIFE

MEDICINES. CHEMISTRY IN EVERYDAY LIFE. Done by Vishal Rajesh Lakhiani 12 - O. INTRODUCTION. Drug – A chemical of low molecular mass (100 – 500u) which interact with macromolecular targets and produce a biological response.

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CHEMISTRY IN EVERYDAY LIFE

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  1. MEDICINES CHEMISTRY IN EVERYDAY LIFE Done by Vishal Rajesh Lakhiani 12 - O

  2. INTRODUCTION • Drug – A chemical of low molecular mass (100 – 500u) which interact with macromolecular targets and produce a biological response. • Medicine – When the biological response produced by a drug is therapeutic and useful, then the drug is called a medicine.

  3. CLASSIFICATION OF DRUGS

  4. ON THE BASIS OF PHARMACOLOGICAL EFFECT • This classification is based on the pharmacological effect of the drugs. It is useful for doctors because it provides them the whole range of drugs available for the treatment of a particular type of problem. • For example, analgesics have pain killing effect, antiseptics kill or arrest the growth of microorganisms.

  5. ON THE BASIS OF DRUG ACTION • It is based on the action of a drug on a particular biochemical process. • For example, all antihistamines inhibit the action of the compound, histamine which causes inflammation in the body. There are various ways in which action of histamines can be blocked.

  6. ON THE BASIS OF CHEMICAL STRUCTURE • It is based on the chemical structure of the drug. Drugs classified in this way share common structural features and often have similar pharmacological activity. • For example, all sulphonamides are derivatives of

  7. ON THE BASIS OF MOLECULAR TARGETS • Drugs usually interact with biomolecules such as carbohydrates, proteins, lipids and nucleic acids. These are called target molecules or drug targets. • Drugs possessing some common structural features may have the same mechanism of action on targets. The classification based on molecular targets is the most useful classification for medicinal chemists.

  8. ENZYMES&RECEPTORS

  9. ENZYMES • Enzymes are biological catalysts. Most are proteins. (A few ribonucleoprotein enzymes have been discovered and, for some of these, the catalytic activity is in the RNA part rather than the protein part. Link to discussion of these ribozymes.) • Enzymes bind temporarily to one or more of the reactants of the reaction they catalyze. In doing so, they lower the amount of activation energy needed and thus speed up the reaction.

  10. ENZYME ACTION • Most of these interactions are weak and especially so if the atoms involved are farther than about one angstrom(10-10m) from each other. So successful binding of enzyme and substrate requires that the two molecules be able to approach each other closely over a fairly broad surface. Thus the analogy that a substrate molecule binds its enzyme like a key in a lock. • This requirement for complementarity in the configuration of substrate and enzyme explains the remarkable specificity of most enzymes. Generally, a given enzyme is able to catalyze only a single chemical reaction or, at most, a few reactions involving substrates sharing the same general structure.

  11. COMPETITIVE INHIBITION • The necessity for a close, if brief, fit between enzyme and substrate explains the phenomenon of competitive inhibition. • One of the enzymes needed for the release of energy within the cell is succinicdehydrogenase. • It catalyzes the oxidation (by the removal of two hydrogen atoms) of succinic acid (a). If one adds malonic acid to cells, or to a test tube mixture of succinic acid and the enzyme, the action of the enzyme is strongly inhibited. This is because the structure of malonic acid allows it to bind to the same site on the enzyme (b). But there is no oxidation so no speedy release of products. The inhibition is called competitive because if you increase the ratio of succinic to malonic acid in the mixture, you will gradually restore the rate of catalysis. At a 50:1 ratio, the two molecules compete on roughly equal terms for the binding (=catalytic) site on the enzyme.

  12. FACTORS AFFECTING ENZYME ACTION

  13. FACTORS AFFECTING ENZYME ACTION • The activity of enzymes is strongly affected by changes in pH and temperature. Each enzyme works best at a certain pH (left graph) and temperature (right graph), its activity decreasing at values above and below that point. Examples: • the protease pepsin works best as a pH of 1–2 (found in the stomach) while • the protease trypsin is inactive at such a low pH but very active at a pH of 8 (found in the small intestine as the bicarbonate of the pancreatic fluid neutralizes the arriving stomach contents).

  14. REGULATION OF ENZYME ACTIVITY • Several mechanisms work to make enzyme activity within the cell efficient and well-coordinated. • Anchoring enzymes in membranes: • Many enzymes are inserted into cell membranes, for examples, • the plasma membrane • the membranes of mitochondria and chloroplasts • the endoplasmic reticulum • the nuclear envelope • These are locked into spatial relationships that enable them to interact efficiently.

  15. INACTIVE PRECURSORS • Enzymes, such as proteases, that can attack the cell itself are inhibited while within the cell that synthesizes them. For example, pepsin is synthesized within the chief cells (in gastric glands) as an inactive precursor, pepsinogen. Only when exposed to the low pH outside the cell is the inhibiting portion of the molecule removed and active pepsin produced.

  16. FEEDBACK INHIBITION • If the product of a series of enzymatic reactions, e.g., an amino acid, begins to accumulate within the cell, it may specifically inhibit the action of the first enzyme involved in its synthesis (red bar). Thus further production of the enzyme is halted.

  17. PRECURSOR ACTIVATION • The accumulation of a substance within a cell may specifically activate (blue arrow) an enzyme that sets in motion a sequence of reactions for which that substance is the initial substrate. This reduces the concentration of the initial substrate.

  18. ALLOSTERIC SITES • In the case of feedback inhibition and precursor activation, the activity of the enzyme is being regulated by a molecule which is not its substrate. In these cases, the regulator molecule binds to the enzyme at a different site than the one to which the substrate binds. When the regulator binds to its site, it alters the shape of the enzyme so that its activity is changed. This is called an allosteric effect. • In feedback inhibition, the allosteric effect lowers the affinity of the enzyme for its substrate. • In precursor activation, the regulator molecule increases the affinity of the enzyme in the series for its substrate.

  19. Graph showing velocity of reaction with concentration of substrate in the presence of an enzyme

  20. The Effects of Enzyme Inhibitors • Enzymes can be inhibited • competitively, when the substrate and inhibitor compete for binding to the same active site or • noncompetitively, when the inhibitor binds somewhere else on the enzyme molecule reducing its efficiency. • The distinction can be determined by plotting enzyme activity with and without the inhibitor present.

  21. COMPETITIVE INHIBITION • In the presence of a competitive inhibitor, it takes a higher substrate concentration to achieve the same velocities that were reached in its absence. So while Vmax can still be reached if sufficient substrate is available, one-half Vmax requires a higher [S] than before and thus Km is larger.

  22. NON-COMPETITIVE INHIBITION • With noncompetitive inhibition, enzyme molecules that have been bound by the inhibitor are taken out of the game so • enzyme rate (velocity) is reduced for all values of [S], including • Vmax and one-half Vmax but • Km remains unchanged because the active site of those enzyme molecules that have not been inhibited is unchanged.

  23. DRUG-RECEPTOR INTERACTIONS • Receptors are proteins that are crucial to body’s communication process. • The vast majority of drugs show a remarkably high correlation of structure and specificity to produce pharmacological effects. Experimental evidence indicates that drugs interact with receptor sites localized in macromolecules which have protein-like properties and specific three dimensional shapes. A minimum three point attachment of a drug to a receptor site is required. In most cases a rather specific chemical structure is required for the receptor site and a complementary drug structure. Slight changes in the molecular structure of the drug may drastically change specificity.

  24. DRUG INTERACTION WITH RECEPTOR SITE • A neurotransmitter has a specific shape to fit into a receptor site and cause a pharmacological response such as a nerve impulse being sent. The neurotransmitter is similar to a substrate in an enzyme interaction. • After attachment to a receptor site, a drug may either initiate a response or prevent a response from occurring. A drug must be a close "mimic" of the neurotransmitter.

  25. AGONIST & ANTAGONIST • An agonist is a drug which produces a stimulation type response. The agonist is a very close mimic and "fits" with the receptor site and is thus able to initiate a response. • An antagonist drug interacts with the receptor site and blocks or depresses the normal response for that receptor because it only partially fits the receptor site and can not produce an effect. However, it does block the site preventing any other agonist or the normal neurotransmitter from interacting with the receptor site.

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