![[object Object],[object Object],¿Como actúan los fármacos? DR. FAUSTO ZARUMA TORREZ](data:image/gif;base64,R0lGODlhAQABAIAAAAAAAP///yH5BAEAAAAALAAAAAABAAEAAAIBRAA7)
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Dinamia cl5.1
- 1. PRINCIPIOS DE FARMACODINAMIA DR. FAUSTO ZARUMA TORREZ
- 4. DR. FAUSTO ZARUMA TORREZ FARMACO Captación y transducción de la señal Modulación de la función Acciones No Deseadas Acciones Deseadas Acciones Tóxicas Selectivas EFECTO ADVERSO EFECTO TERAPEUTICO
- 6. DR. FAUSTO ZARUMA TORREZ F R F R E E RESPUESTABIOLOGICA Flujo de iones Activación o inactivación de enzimas Síntesis proteica Liberación de NT Reconocimiento Acoplamiento Transducción Amplificación Interacción Fármaco Receptor
- 8. DR. FAUSTO ZARUMA TORREZ
- 10. DR. FAUSTO ZARUMA TORREZ
- 11. DR. FAUSTO ZARUMA TORREZ
- 12. DR. FAUSTO ZARUMA TORREZ
- 14. DR. FAUSTO ZARUMA TORREZ RECEPT. ACOPLADOS A LIGANDO
- 15. DR. FAUSTO ZARUMA TORREZ
- 16. CANALES IONICOS Y DOMINIOS DR. FAUSTO ZARUMA TORREZ
- 17. RECEPTORES CON ACTIVIDAD ENZIMATICA DR. FAUSTO ZARUMA TORREZ
- 18. DR. FAUSTO ZARUMA TORREZ
- 19. Familias de Receptores III DR. FAUSTO ZARUMA TORREZ D. FACTORES DE TRANSCRIPCION: Hormonas esteroidales, tiroideas, etc.
- 20. Tipos de Enlaces Fármaco-Receptor DR. FAUSTO ZARUMA TORREZ
- 21. DR. FAUSTO ZARUMA TORREZ
- 22. DR. FAUSTO ZARUMA TORREZ
- 23. DR. FAUSTO ZARUMA TORREZ
- 24. DR. FAUSTO ZARUMA TORREZ
- 26. Cinética de la Interacción Fármaco-Receptor DR. FAUSTO ZARUMA TORREZ KD es la cantidad de fármaco necesaria para provocar el 50% del efecto máximo (dosis activa 50 o DA50). En términos de efecto:
- 28. Teoría de los Estados Conformacionales DR. FAUSTO ZARUMA TORREZ Agonista Total: Afinidad solo por RA Agonista Parcial: Afinidad RA > Afinidad RI Antagonista: Afinidad RA = Afinidad RI Agonista Inverso: Afinidad RA < Afinidad RI
- 34. DR. FAUSTO ZARUMA TORREZ
Notas del editor
- Types of Binding Forces Unless a drug comes into contact with intrinsic structures of the body, it cannot affect body function. Covalent bond. Two atoms enter a covalent bond if each donates an electron to a shared electron pair (cloud). This state is depicted in structural formulas by a dash. The covalent bond is “ firm”, that is, not reversible or only poorly so. Few drugs are covalently bound to biological structures. The bond, and possibly the effect, persist for a long time after intake of a drug has been discontinued, making therapy difficult to control. Examples include alkylating cytostatics (p. 298) or organophosphates (p. 102). Conjugation reactions occurring in biotransformation also represent a covalent linkage (e.g., to glucuronic acid, p. 38). Noncovalent bond. There is no formation of a shared electron pair. The bond is reversible and typical of most drug-receptor interactions. Since a drug usually attaches to its site of action by multiple contacts, several of the types of bonds described below may participate. Electrostatic attraction (A). A positive and negative charge attract each other. Ionic interaction: An ion is a particle charged either positively (cation) or negatively (anion), i.e., the atom lacks or has surplus electrons, respectively. Attraction between ions of opposite charge is inversely proportional to the square of the distance between them; it is the initial force drawing a charged drug to its binding site. Ionic bonds have a relatively high stability. Dipole-ion interaction: When bond electrons are asymmetrically distributed over both atomic nuclei, one atom will bear a negative (δ–), and its partner a positive (δ+) partial charge. The molecule thus presents a positive and a negative pole, i.e., has polarity or a dipole. A partial charge can interact electrostatically with an ion of opposite charge. Dipole-dipole interaction is the electrostatic attraction between opposite partial charges. When a hydrogen atom bearing a partial positive charge bridges two atoms bearing a partial negative charge, a hydrogen bond is created. A van der Waals’ bond (B) is formed between apolar molecular groups that have come into close proximity. Spontaneous transient distortion of electron clouds (momentary faint dipole, δδ) may induce an opposite dipole in the neighboring molecule. The van der Waals’ bond, therefore, is a form of electrostatic attraction, albeit of very low strength (inversely proportional to the seventh power of the distance). Hydrophobic interaction (C). The attraction between the dipoles of water is strong enough to hinder intercalation of any apolar (uncharged) molecules. By tending towards each other, H2O molecules squeeze apolar particles from their midst. Accordingly, in the organism, apolar particles have an increased probability of staying in nonaqueous, apolar surroundings, such as fatty acid chains of cell membranes or apolar regions of a receptor.