Drug Target (Part 1)

• A molecule in the body that is intrinsically associated with a particular disease process and that could be addressed by a drug to produce a desired therapeutic effect

  Drug Target
• specialized class of proteins responsible for catalyzing chemical reactions within the cell to sustain life

  Enzymes
• Lock and Key was first potulated by _____ in____

  Emil Fischer; 1894
• A theory wherein enzymes and substrates must have complimentary shapes in order for catalysis to occur

  Lock and Key
• An area that permits thebinding of specific molecules or substrates during reaction or catalysis

  Target site
• A theory wherein the active site of enzymes and the substrate do not have the same shape but the enzyme active site reshapes in response to substrate binding

  Induced Fit
• Induced Fitwas proposed by _____ in ____

  Daniel Koshland; 1958
• Ability of enzymes to be therapeutically modulated or affected by drugs

  Druggability
• How many percent of drugs in the market target enzymes?

  47%
• It describes how restrictive enzymes are in selecting its substrates

  Specificity
• Reversible inhibitors form _____ with the enzyme

  non-covalent bonds
• A process wherein the activity of an enzyme is regulated or hindered

  Enzyme Inhibition
• The activity of an enzymes is regulated or hindered by the presence of a molecule called an _____

  inhibitor
• This are very weak bonds

  Hydrophobic bonds
• Bonds of electronegative atoms like Sulfur, Oxygen, Nitrogen that is present in FG

  Hydrogen bonds
• They can act across long distances and are reversible

  Ionic bonds
• Types of reversible inhibition

  competitive; non-competitive; uncompetitive
• A type of reversible enzyme inhibition where substrate and inhibitor compete in binding with the active site

  competitive
• A type of reversible enzyme inhibition wherein the inhibitor binds in the area other than the active site

  non-competitive
• The area where the inhibitor binds other than the active site is called

  allosteric site
• Counteract the effects of the inhibitor

  allosteric modulators
• What does acetazolamide inhibit?

  carbonic anhydrase
• How can you overcome competitive and non-competitive inhibition?

  increasing substrate concentration
• A type of reversible enzyme inhibition wherein the inhibitor binds with the complex of substrate and enzyme

  uncompetitive
• Uncompetitive enzyme inhibition can be overcomed by

  alteration of enzyme reaction conditions
• Lithium used for treating bipolar inhibits the actions of _____ in the body

  inositol
• A type of enzyme inhibition wherein covalent bods are involved

  irreversible
• Irreversible enzyme inhibition is also called

  suicide inhibition
• Irreversible enzyme inhibition can be overcomed by the

  synthesis of new enzymes
• What does clavulanic acid inhibit?

  Beta-lactamase
• Activator binds to the active site to change its shape in order for the substrate to bind

  enzyme activation
• It activates glucokinase/hexokinase to increase the production of glucose to G6P in diabetic patients

  piragliatin
• Comprise only _% of the drugs in the market target nucleic acids

  1
• Inhibit the synthesis of nucleic acids

  antimetabolites
• It is an anticancer drug that inhibit dihydrofolate reductase

  methotrexate
• These are cresent-shaped and they form strong complexes with the grooves of DNA


  groove binders
• It is a drug under groove binders that disrupts the cancer cell

  distamycin
• These are cationic, aromatic, planar polycyclic systems that interacts with DNA through non-covalent π-π interactions

  intercalators
• It disrupts DNA synthesis and prevent bacterial production

  Proflavine
• These introduce themselves in DNA during replication and cease chain growth

  chain terminators