Lecture

Covalent Inhibitors Kinetics

Graph Chat

Chat with Graph Search

Ask any question about EPFL courses, lectures, exercises, research, news, etc. or try the example questions below.

DISCLAIMER: The Graph Chatbot is not programmed to provide explicit or categorical answers to your questions. Rather, it transforms your questions into API requests that are distributed across the various IT services officially administered by EPFL. Its purpose is solely to collect and recommend relevant references to content that you can explore to help you answer your questions.

Description

This lecture discusses the kinetics of covalent inhibitors, focusing on compounds A and B. The instructor explains the two-step binding regimen of compound A and the direct alkylation inhibition mechanism of compound B. The lecture covers the derivation of second-order rate constants and specificity of binding. Various experiments to demonstrate the covalent nature of the inhibitors are explored, along with the interaction of the inhibitors with a small-molecule thiol. The session concludes with a scheme illustrating how compounds A and B interact with a cysteine within the protein, considering the impact of oxidation on non-covalent interactions.

This video is available exclusively on Mediaspace for a restricted audience. Please log in to MediaSpace to access it if you have the necessary permissions.

Watch on Mediaspace

Official source

Related concepts (32)

Enzyme inhibitor

An enzyme inhibitor is a molecule that binds to an enzyme and blocks its activity. Enzymes are proteins that speed up chemical reactions necessary for life, in which substrate molecules are converted into products. An enzyme facilitates a specific chemical reaction by binding the substrate to its active site, a specialized area on the enzyme that accelerates the most difficult step of the reaction.

Enzyme kinetics

Enzyme kinetics is the study of the rates of enzyme-catalysed chemical reactions. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or a modifier (inhibitor or activator) might affect the rate. An enzyme (E) is typically a protein molecule that promotes a reaction of another molecule, its substrate (S).

Chemical kinetics

Chemical kinetics, also known as reaction kinetics, is the branch of physical chemistry that is concerned with understanding the rates of chemical reactions. It is different from chemical thermodynamics, which deals with the direction in which a reaction occurs but in itself tells nothing about its rate. Chemical kinetics includes investigations of how experimental conditions influence the speed of a chemical reaction and yield information about the reaction's mechanism and transition states, as well as the construction of mathematical models that also can describe the characteristics of a chemical reaction.

Protein–protein interaction

Protein–protein interactions (PPIs) are physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that occur in a cell or in a living organism in a specific biomolecular context. Proteins rarely act alone as their functions tend to be regulated.

Chemical specificity

Chemical specificity is the ability of binding site of a macromolecule (such as a protein) to bind specific ligands. The fewer ligands a protein can bind, the greater its specificity. Specificity describes the strength of binding between a given protein and ligand. This relationship can be described by a dissociation constant, which characterizes the balance between bound and unbound states for the protein-ligand system.

Related lectures (44)

Enzymes: Basic Concepts and Kinetics

Delves into enzymes' basic concepts, kinetics, and catalytic strategies for reaction acceleration.

Reaction Kinetics: Temperature Influence

Discusses temperature's impact on reaction rates, activation energy, collision efficiency, reaction mechanisms, catalysis, and enzymatic catalysis.

Kinetics: Reaction Rates and Equilibrium

Explores reaction kinetics, rate laws, measurement techniques, and binding kinetics between ligands and proteins.

Microbial Growth: Understanding Environmental Microbiology

Covers microbial growth principles, enzyme kinetics, and the impact of nutrient limitations in environmental microbiology.

Enzyme Kinetics: Understanding Reaction Rates and Mechanisms