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193 Cards in this Set

  • Front
  • Back
What are natural products? What are they also referred to as?
Chemical compounds extracted from flora and fauna.Referred to as secondary metabolites.
Collections of naturally occurring chemical compounds generally have what kind of properties?
drug-like properties, since they are derived from a living organism.
What kind of resource are natural products?
Natural products are a finite resource, and disappearance of natural chemical sources through overpopulation may result in a loss of important unrecorded chemical information.
What is Pharmacognosy? What does it involve?
Is the multidisciplinary study of drugs of natural origin as well as the search for new drugs of natural origin. Involves many sciences: ethnobotany, biology, chemistry.
What are synthetically produced chemical drug compounds? Why are they used?
Chemical drugs that are synthesized to approximate the physiochemical properties of natural products. This way, the drug candidate has a greater chance of being developed into a medicine for human use.
Why are the physiochemical properties of a drug adjusted?
The physiochemical properties of a drug can be adjusted chemically in order to ensure the drug interacts with the body in a consistent manner.
What are the four physiochemical properties?
pKa, logP, solubility, polarity.
What are the 5 approaches to choosing plants and animals?
Random screening, selection of specific taxonomic groups, Chemotaxonomic (restricted classes of secondary metabolites sought (eg alkaloids)), information managed (database surveillance gives clues to fruitful organisms), Ethnomedical (ethnobotanical advice collected from local cultures leads to the identification of source organism).
Organisms for natural product discovery work may be classified in what 6 kingdoms?
Eubacteria, Archaea, Protoctista, Plantae, Fungi, Animalia
What are initial extracts of Natural Products from Organism?
Samples of collected organic material are extracted and purified using a variety of basic laboratory and biochemical techniques
What are the 4 steps of isolation of natural products from an organism?
1.Collect sample from the environment
2. Extract the sample between solvents (water/organic)
3. Filter and concentrate solvent to get crude chemical mixture.
4.Test crude mixture in assay, or purify the sample using chromatography.
What is Liquid Chromatography (LC) used for?
is used to identify specific active ingredients in the extract mixture.
What is Chromatography based on?
Chromatography is based on the differential adsorption of mixture components on a variety of stationary phases (Sephadex, alumina, silica) while eluting with normal phase and reverse phase solvent systems.
What is High Throughput Screening (HTS) used for?
Crude extracts containing a mix of chemical compounds are often tested in a High Throughput Screening (HTS) Assay
What are cell based assays?
whole cells are treated with the chemical extract and one of the cellular processes (cell products) is monitored for change. It offers more information on biological relevance, since it is affecting a small living entity, BUT is harder to run in an automated laboratory.
What is an Enzymatic Assay?
a specific enzyme is treated with the chemical extract and monitored for change. Easier to achieve in automated laboratory, but less direct info on the usefulness of the chemical extract in a living organism.
What does Mass Spec (MS) give?
gives exact chemical mass and very useful for structure determination – the way a molecule degrades indicates how it is put together.
What does Nuclear Magnetic Resonance (NMR) supply?
Supplies very detailed structural information
What is X-Ray Diffraction used for?
x-rays are used to analyze a crystallized sample. This gives an accurate 3-D structure.
What does dereplication involve?
Dereplication involves the checking of active natural extracts against known active components BEFORE purification occurs, in order to prevent RE-discovery of previous active components.
What is a Metabolome?
– is a snapshot of the physiology of a cell, including metabolites present after cell processes occur. Imagine freezing a cell and peering at all the chemical structures in detail. This gives us an idea of the chemical processes occurring within the cell.
What does Structure-Activity Relations (SAR) involve?
Involves chemical manipulation of the molecule in a systematic fashion and the determination of how these changes affect biological activity.
What do functional groups within a molecule contribute?
contribute in an additive manner to the physiochemical properties and thus biological action of that molecule.
To treat pathophysiologic condition we must have knowledge of what two components?
we must have knowledge of the effect of the drug’s mechanism, as well as physicochemicalproperties of the molecule
What does Physicochemical refer to?
refers to the influence of specific functional groups within the molecule on it’s acid-base properties, solubility, partition coefficient, and so on…
What is target identification?
Identifying a biological mechanism that may be regulated in order to prevent sickness or disease.
What is target validation?
Developing an enzyme assay or test that can quantify how well a drug works to regulate the biological mechanism.
What is Lead Identification?
Identifying a unique chemical structure (drug candidate) that works to regulate the biological mechanism.
What is Lead Optimization?
Systematically changing the chemical structure in order to make a drug candidate more potent, more selective, and safe for human dosing
What is preclinical development?
Producing large quantities of the improved drug candidate in pure form and properly formulated for dosing.
What is clinical development?
Dosing the drug in humans in order to determine safety and efficacy in the patient population.
How long does it take at the minimum to put a drug out?
8 years
What does pKa indicate?
indicates the relative
acid/base strength of a functional group and it also allows the
calculation of the percent ionization of a functional group at a
given pH.
What is the pH scale? What is the equation?
logarithmic, relationship to H+ ion conc. pH= -log[H¬+]
What is the pOH scale? What is the equation?
also logarithmic, but referencing OH- ion. pH + pOH = 14
What is the pKa scale?
logarithmic, relationship to ratio of acid/base and pH
Do strong acids and bases completely dissociate in water? What do they produce?
produce their respective acids and bases almost completely, shifting the equilibrium to the right. pKa for strong acids is <1 (essentially no ionization constant)
What is the Bronsted-Lowry Acid Base Theory?
Acid is something that donates a proton (H+). Base is something that accepts a proton(H+).
The pKa is a constant that is specifi to what?
specific to a functional group and is an indicator of its behavior as an acid or base in an aqueous environment.
pKa can be used with the pH to determine what?
to determine the percent of a functional group that is ionized using the Henderson-Hasselbalch equation
What is the henderson hasselbalch equation?
pka= pH+log [acid]/[base]
What is the water solubility of a small organic molecule determined by?
determined by the hydrogen bond forming potential and the degree of ionization of a molecule.
What kind of interactions are hydrogen bonds?
Hydrogen bonds are dipole-dipole interactions between a partial negative charge heteroatom (usually nitrogen or oxygen) and a partial positive charge hydrogen atom.
What do carbons and structures which do not form hydrogen bonds add?
add to the “greasiness” of a molecule, and act to make the molecule more “hydrophobic” (“water-hating”).
When molecules are in a solution at a certain pH, what can we determine?
determine the degree of ionization (Henderson Hasselbalch)
What else forms hydrogen bonds? Why is this done?
Ionized functional groups may ALSO form hydrogen bonds, so that solubility MAY improve when they are in “salt form”.
What is the LogP, partition coefficent, based on?
based on experimental solubility data of small organic molecules between octanol (“non-polar organic”) and water (“polar aqueous”) solvents.
What is Lipinski's rule of 5?
1. Not more than 5 hydrogen bond donors
2. Not more than 10 hydrogen bond acceptors.
3. a molecular weight under 500 daltons.
4. An octanol-water partition coefficient logP of less than 5
What are enantiomers?
describes the relationship between two chiral compounds that are non-superimposable mirror images
What are diastereomers?
describes the relationship between two chiral compounds that are non-superimposable NON-mirror images
Enantiomers have the same what?
Enantiomers have the same physicochemical properties.
How can Enantiomers be separated?
can only be separated chemically by using a chiral chromatography column or chiral environment.
Diastereomers have different what? Can they be separated?
different physicochemical properties and can be chemically separated from one another more easily.
Once drugs are in the body, what kind of environment are they in?
they are in a CHIRAL environment and so the correct stereochemistry of the drug is essential for drug action.
Define racemic.
a mixture of two enantiomers, where one enantiomer is active and the other is not.
What is Cahn-Ingold- Prelog (CIP) nomenclature?
The absolute configuration is the priority sequence of R (“right”) or S (“left”) turning substituents on a chiral center as based on atomic weight - the higher the atomic weight, the higher the assigned priority.
What is the Easson-Stedman hypothesis? What does the more potent enantiomer have compared to the weaker one?
The hypothesis that reasons that the differences in biological activity between enantiomers is due to the molecules’ “fit” to the receptor. The more potent enantiomer has at least three (3) molecular interactions with the receptor, whereas the less potent enantiomer interacts with only two (2) sites.
Conformation Isomers differ only how? What does this result in?
Conformational isomers differ only by the rotation of a single bond, which results in many slightly different conformations, which can bind to different receptors in a biological system.
What does the gauche form of acetylcholine bind to? What does the achiral form bind to?
binds to a nicotinic receptor whereas the anti- form (achiral) binds to a muscarinic receptor.
What is lead discovery?
which is the identification of a chemical structure that is a good STARTING POINT for chemical refinement and modification.
The discovery of new lead compounds can occur through what 5 techniques?
1. Natural Product screenng
2.Random Screening
3.Target dedicated screening and rational design.
4. Drug Metabolism Studies
(The metabolites of a drug can have pharmacological effect, and these altered chemical structures may provide a starting point for chemical modification.)
5. Side Effect Observations
(Side effects point to different pharmacological routes for a biologically-degraded chemical structure. Sometimes this alternate effect provides a good starting point for development of new SAR, which leads to a new drug candidate.)
What is the pharmacophore?
The pharmacophore is the portion of a drug molecule containing the essential organic functional groups that interact directly with the receptor active site and confer its biological activity.
What is Isosterism?
when similar functional groups have similar properties. The replacement of one group for another is “isosteric replacement”.
What is boisosterism?
when similar functional groups have similar biological effects. This can be divided into “classical” and “nonclassical” modifications of the chemical structure.
What are monovalent bioisosteres?
F,H
OH,NH
F, OH, NH OR CH3 for H
SH, OH
CL,Br, CF3
What are Divalent bioisosteres?
-C=S
-C=O
-C=NH
-C=C-
What are trivalent atoms or groups?
-CH=
-N=
-P=
-As=
What do classical groups adhere to?
Classical groups adhere to the tenets of Langmuir and Grimm, and thus have similar arrangements of valence electrons.
What are the 5 classical groups?
Monovalent atoms and groups Divalent atoms and groups Trivalent atoms and groups Tetrasubstituted atoms Ring equivalents
What are the 2 nonclassical groups?
Exchangeable groups Rings vs. noncyclic structure
Classical bioisosteres retain what?
retain most of the shape and connectivity of the original structure.
Non Classical bioisosteres mimic what?
may just mimic spatial arrangement, physicochemical properties, or electronic properties of the original.
What does the Schrödinger equation relate?
relates the energy of the system to the quantum-mechanical wavefunction of the system
what is this equation k*(x-x0)^2?
Hooks Law. K is the force constant, x0 is the equilibirum bond length, x is whatever value the bond length has
In Hookes law what are the force field parameters in the energy equation?
K and x0
What do K and x0 determine in Hooke's law?
determine, respectively, how quickly the bond gets longer and shorter, and what the preferred distance between the two constituent atoms is; k is an energetic parameter and x0 is a geometric parameter
If the force field parameters differ depending on the constituent atoms how will C-C bond's K and x0 differ from a C=C bond?
C-C bond will have a smaller k and a larger x0 than a C=C bond
How do we get force field parameters?
Experimental data and data from quantum mechanical models
What are benefits of molecular mechanics?
1. Much much much less computationally expensive than quantum mechanical models, allowing the study of systems of biomolecular interest such as DNA, membrane proteins, and protein:small-molecule binding
What are energy minimization algorithms used for?
iv. Can be used to “geometry optimize” a chemical structure (e.g. relieve strain in stretched bonds and distorted angles)
What are molecular dynamics simulation used for?What does it stimulate?
Used for calculation of time-averaged properties: structure, energy, conformation. Simulates the movement of all atoms in a molecule
What can Monte Carlo Simulation impose?
Can impose relatively large motions on the system and then determine whether the altered structure is energetically feasible.
What can't Monte Carlo Simulation provide?
Cannot provide time-dependent quantities
What are receptor based virtual screenings goal?
i. Goal is to find a small molecule (from a database of thousands to millions of compounds) that binds a target protein in a particular fashion given the protein’s three-dimensional structure
What are the 2 most general natures of drug action?
Killing foreign organisms and Stimulation or Depression of normal physiological function.
Describe the process of killing a foreign organism? What is the principle action?
Chemotheraputic agents act by killing or weakening foreign organisms such as bacteria, worms, viruses. The principle of action is selective toxicity, where the drug is more toxic to the parasite than the host.
What are the three ways to group drugs?
By therapeutic use (our curriculum and useful in practice/specialty)
By Chemical structure ( can make identifications of same drug class, always part of medchem perspective)
By Mechanism of Action ( most useful for discussions of biochem)
What is the first step in a drug development project?
Grouping by MOA
Define "actions" of a drug.
the physiological biochemical mechanisms by which a chemical produces a response in living tissues.
Define the drug's "Effect"
The observable consequence of drug action.
What are the types times of Drug Actions?
At a receptor (cell membrane), at an enzyme(anywhere in the body, can have sites of receptors on them) and non-specific interactions.
What are examples of 3 non-specific interactions?
Antacids--> Increase pH of stomach
Diuretics--> creates osmotic potential in renal tubules and foster water elimination.
EDTA--> Chealting agent in high affinity for Pb+
Define a receptor?
A chemical binding pocket that interacts with a ligand (drug) at the molecular level.
In biochemistry what is a receptor defined as?
a receptor is a protein molecule embedded in either the plasma membrane or the cytoplasm of a cell to which one or more specific kinds of signaling molecules may attach.
Each kind of receptor can only bind certain what?
ligand shapes
Interaction of receptor with the ligand may depend on what types of chemical bonding?
Covalent (strongest, irreversible)
Ionic
Hydrogen
Hydrophobic interactions (greasiness and association of non-polar groups)
In Ionic bonding, when does strength decrease?
with the square of distance
What is the idea of Affinity Conformation?
How conformational changes in the receptor are thought to effect binding of ligand.
What is the Occupancy theory?
intensity of the biological response directly related to number of receptors bound by agonist
What is the rate theory?
intensity of the response determined by the number of drug-receptor interactions per unit time. Rapid association/dissociation of ligand makes for a robust response.
What is the induced fit theory?
receptor changes conformation to allow better fit of ligand (describes antagonism/agonism)
What is the macromolecular perturbation theory?
two types of receptor conformational changes exist – agonistic and antagonistic (describes antagonism/agonism/partial agonism
What is the activation-aggregation theory?
receptors are always in dynamic equilibrium between active and inactive states (describes antagonism/agonism/partial agonism/inverse agonism)
What are the three affects of binding of a ligand?
1. The three dimensional characteristics of a molecule need to be perfect into produce agonism.
2. When drugs contain stereocenters there is an added cost and complexity to their production.
3.c. When prepared drugs are a mixture of enantiomers, the properly fitting enantiomer is helpful as a pharmaceutical agent, but the opposite enantiomer may be either uninvolved or toxic.
State is a Eutomer? what state is a Distomer?
Active.
Inactive or worse
Why is receptor binding used in drug discovery?
to screen large collections of chemical compounds versus a particular receptor.
What does drug + receptor give?
Biological response
What are dose-response relations plotted to determine?
qualitative and quantitative parameters of potency and efficacy
What is potency?
is inversely related to the dose required to produce a given response (typically 50% maximum).
What is efficacy?
is the ability of a drug to produce a full response (100% of maximum)
Nerve Cell: Presynaptic and Postsynaptic Receptors may do what? Why do they do that?
self-regulate their activity due to the fact that neurotransmitters can serve a secondary function modulating their own release.
What is labetalol a combination of? What is RR sterochemistry major activity for? What is SR major sterochemistry for?
alpha and beta adrenoceptor blocker.
B-adrenoreceptor
Alpha-adrenoreceptor
The rate theory is ___ dependent?
time
What determines the biological rate?
Amount of receptors that are on.
In the induced fit theory, assume native conformation is not proper for binding . When not associating with agonist, what does the receptor do? What else may bind to by induced fit?From this what is not elicited?
Receptor reverts to its original conformation.
Antagonist.
No biological response.
In the Macromolecular perturbation theory when two types of receptor conformational changes exist: agonistic and antagonistic, what does the rate of their existence determine?
biological response
Agonist function by shifting the equilibrium towards what? What does the antagonist shift the equilibrium toward?
Toward the active state.
Toward the inactive state.
What happens in signal transduction?
Cell converts an and transmits extracellular signal into the interior of the cell.
What does signal transduction enable?
extracellular molecules to affect cell function w/o entering cell. Several signals may affect one another and help cell to respond to multiple stimuli
During signal transduction, what may happen to a weak signal?
A weak signal may be amplified and made robust by enzyme activation and second messengering.
What are three Transmembrane Ion Channels?
Ligand-Gated
Volatage-Gated
Second Messenger Gated
What are the 4 major families of receptors that are capable of interacting withing the body?
Transmembrane Ion Channels
Transmembrane G-protein coupled Transmembrane catalytic receptors
Intracellular Cytoplasmic/Nuclear Receptors
What kind of speed does Ligand-Gated act at? Why does it act like this? What kind of signaling are they important for?
fast acting, because they require only the activation of a single molecule. Important for nerve and muscle signalling
What does a volt across a membrane cause?
changes within cell
What can open or close an ion channel? What are 2 examples?
secondary messengers such as cAMP and IP3 can act to open or close an ion channel
What are Transmembrane G-protein coupled receptors a family of? They have a well conserved structure and signal via what?What do a variety of second messenger products and pathways result from?
a family of multi-subunit transmembrane proteins which have a well conserved structure and signal via the activation of intracellular “G-proteins”. A variety of second messenger products and pathways result from GPCR signaling.
What kind of sites, structures and activity do trans-membrane catalytic receptors have? How are they activated?
monomeric structures with an extracellular catalytic site and intracellular structure with enzymatic activity. Primarily activated by hormones.
Enzyme-coupled receptors have the same sites, structures and activity as trans-membrane catalytic receptors have but what do they bind to?
bind to separate enzymatic proteins for activation
What are Intracellular Cytoplasmic /Nuclear receptors not associated with? Where are they located or bound to?
NOT associated with the plasma membrane, but are located in the cytoplasm or bound to the surface of the nucleus.
What are Intracellular Cytoplasmic / Nuclear receptors composed of? What are they activated by and why? What does this activation cause?
Composed of a single polypeptide with three functional domains. Activated by lipid-soluble ligands, because they must passively diffuse through the lipid cell membrane. Thus, there is a SLOW signal response time.
When can a partial agonist function as an antagonist
When it interferes with the ability of a full agonist to bind
In the absence of agonist, however, the partial agonist only displays what?
agonist activity
In order to maintain homeostasis, what must an organism constantly do?
constantly adapt the numbers/sensitivity of receptors in response to the changing environment in the vicinity of the receptor.
An organism may regulate or alter what?
may regulate the concentration of an enzyme in a particular location, or may alter the rate of synthesis or degradation of receptors as well.
Chromic administration of antagonists/agonists may cause what?
agonists may cause receptor adaptation which might make termination of treatment dangerous.
What are the 9 Receptor classes?
Adrenoceptors, Dopamine receptors, Excitatory amino acid receptors, GABA receptors, Histamine receptors, Muscarinic receptor, Nicotinic receptor, Opioid receptor, Serotonin receptors (5-HT)
What subtypes are associated with Adrenoceptors?
a1, a2, B1, B2
What subtypes are associated with Dopamine receptors?
D1, D2
What subtypes are associated with Excitatory amino acid receptors?
NMDA, AMPA, Kainate
What subtypes are associated with GABA receptors?
GABAa, GABAb
What subtypes are associated with Histamine receptors?
H1, H2
What subtypes are associated with Muscarinic receptors?
M1, M2
What subtypes are associated with Nicotinic receptors?
Nmuscle, Nnauronal,
What subtypes are associated with Opioid receptors?
Mu, Delta, Kappa
What subtypes are associated with serotonin receptors?
5-HT1a, 5-HT2a
Enzyme Mechanisms are what kind of catalysts? Vast majority are what?
Biological Catalysts. Vast majority are proteins (certain RNAs – in ribozymes – are catalytic also)
Like all catalysts, enzymes have the power to do what? What does this result in?
to lower the activation energy of reactions resulting from stabilization of reacting intermediates
Enzymes have what kind of enhancments?
Huge rate enhancements (gauged as “proficiency” of the enzyme)
Enzymes display specificity for what?
chemical bonds, functional groups, or even a single molecule
What are 6 types of reactions that are catalyzed?
Oxidoreductases, transferases, hydrolases, lysases, Isomerases, Ligases/Synthetases
What does oxidoreductases catalyze the transfer of?
catalyzes the transfer of electrons from one molecule to another.
What does Transferases catalyze
catalyzes the transfer of a functional group (e.g., a methyl or phosphate group) from one molecule (called the donor) to another (called the acceptor).
Hydrolases is what kind of reaction? AKA what? In Biochemisty, a hydrolase is an enzyme that catalyzes what?
Hydrolytic reaction. (e.g. esterases) catalyzes the hydrolysis of a chemical bond.
Lysases is the formation or removal of what? AKA what? In biochemistry, a lyase is an enzyme that catalyzes what?
Double Bond.(e.g. hydratase)
Catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure.
Isomerases is AKA what? In biochemistry, an isomerase is an enzyme that catalyzes what?
(e.g. mutarotation by mutases). Ehe structural rearrangement of isomers. Isomerases thus catalyze reactions of the form.
Ligases/Synthetases is an enzyme that can catalyze what?
the joining of two large molecules by forming a new chemical bond, usually with accompanying hydrolysis of a small chemical group dependant to one of the larger molecules.
what is this reaction an example of: A– + B → A + B–?
Oxidoreductases
What is this reaction an example of:
A–X + B → A + B–X?
Transferases
What is this reaction an example of:
A–B + H2O → A–OH + B–H?
Hydrolases
How do Lysases differ from other enzymes?
in that they only require one substrate for the reaction in one direction, but two substrates for the reverse reaction
What is this reaction an example of:
ATP → cAMP + PPi?
Lyases
What is this reaction an example of:
A → B
where B is an isomer of A.
Isomerases
What are these reactions an example of:

Ab + C → A–C + b
or sometimes
Ab + cD → A–D + b + c
Ligases/Synthetases
DNA ligase, an enzyme commonly used in molecular biology laboratories to do what?
to join together DNA fragments.
Enzymes are almost always associated with one or more what?
cofactors– small molecules or ions – that aid in their function.
Who first proposed that enzymes stabilize the active complex through tight binding
Linus Pauling
What is used for those enzymes eliminating water?
'Dehydratase'
In cases where the reverse reaction is the more important, or the only one to be demonstrated what name may be used?
'synthase'
What are noncovalent interactions of enzymes categorized as?
Proximity, Orientation, desolvation and transition state electrostatic stabilization
Covalent Interactions of Enzymes are categorized as what?
Acidic, Basic, Nucleophilic
Once knowledge of a particular enzymatic pathway is determined and the mechanism and kinetics worked out, the challenge is to what?
design a suitable inhibitor that selectively inhibits the enzyme.
Inhibition of enzymes may be categorized as what 2 things?
Reversible or Irreversible
Reversible Enzyme inhibition does not imply what? In many instances, covalent bond formation occurs but what happens to these bonds?
Noncovalent bond formation.
Bonds are hydrolyzed to regenerate free enzyme and inhibitor.
In Reversible Enzyme Inhibition there are instances of _____ of a reversible inhibitor where kinetically it behaves as if it _______ and is ______
Tight Binding, Loses all activity and is irreversibly inhibited
Most rationally designed and clinically useful reversible inhibitors are ______
competitive inhibitors.
Antimetabolites – interfere with the function of what?
of an essential metabolite and slow or stop a molecular process in an organism.
Transition-State Analogues are enzymes that do what?
mimic the substrate portion of the hypothetical transition state of an enzymatic reaction.
Irreversible Enzyme Inhibition is commonly associated with what? The Enzyme cannot be ___?
Bond formation between inhibitor with enzyme.
Enzyme cannot be regenerated.
What are affinity labels?
Are indiscriminate chemical functional groups that will react with any nucleophilic amino acid residue. Or anything nucleophilic, for that matter.
Active Site-Directed Irreversible Inhibitors are enzyme inhibitors that are what?
are tethered to an affinity functional group and will “tie up” an enzyme in this fashion.
Mechanism-Based Irreversible Enzyme Inactivators are what? What are they also known as?
Inherently unreactive chemicals that become very reactive once acted upon by a normal enzymatic process. “suicide substrates”
Mechanism-Based Irreversible Enzyme Inactivators (suicide substrates) must have what 5 specificitys desired?
1.Inactivation should be time dependent (reaction should be irreversible)
2.kinetics should be first order
3.the enzyme should show saturation phenomenon
4.the normal substrate should be able to protect the enzyme against the suicide substrate
5.stoichiometry of the reaction should be around 1:1 (one active site to one inhibitor)
What is this called?
Halo Enol Lactones
What is the name of this?
Clauvulinic Acid
What is molecule named?
Gabaculin
What is this molecule named?
Finasteride
Which graph is a competitive inhibitor?
Which graph is a noncompetitive inhibitor?
Top is Comp

Bottom is noncomp
This picture shows inhibitors of what?

What is this a derivative of?
Inhibitors of HIV Reverse Transcriptase

AZT - thymidine derivative
What is this inhibition of?
Inhibition of Acetycholinesterase
What is this inhibition of?
Inhibition of Acetycholinesterase
What is this inhibitors of?

What is this molecule and what is its cofactor?
Inhibitors of Angiotensin- Converting Enzyme (ACE)

carboxypeptidase having a zinc cofactor
What kind of analogue does this show?

What is the name of this?
Transition-State Analogues

Adenosine deaminase
What kind of inhibitors are these?
Active Site-Directed Irreversible Inhibitors