Affinity Labeling
Roger L. Lundblad in Chemical Reagents for Protein Modification, 2020
Affinity labeling is a technique for the specific modification of an amino acid residue in a protein which involves both the binding of the reagent (affinity label) on the basis of biological specificity and subsequent modification of an amino acid residue through the formation of a covalent bond. There are therefore at least two separate and distinct steps in the process of affinity labeling regardless of whether one is concerned with modification of an enzyme catalytic site or a binding site on a protein not involved in catalysis: the process of specific (selective) binding and the process of covalent bond formation.
Affinity Labeling
Roger L. Lundblad, Claudia M. Noyes in Chemical Reagents for Protein Modification, 1984
Affinity labeling is a technique for the specific modification of an amino acid residue in a protein which involves both the binding of the reagent (affinity label) on the basis of biological specificity and subsequent modification of an amino acid residue through the formation of a covalent bond. There are therefore at least two separate and distinct steps in the process of affinity labeling regardless of whether one is concerned with modification of an enzyme catalytic site or a binding site on a protein not involved in catalysis: the process of specific (selective) binding and the process of covalent bond formation.
Affinity Labeling
Roger L. Lundblad, Claudia M. Noyes in Chemical Reagents for Protein Modification, 1984
Affinity labeling is a technique for the specific modification of an amino acid residue in a protein which involves both the binding of the reagent (affinity label) on the basis of biological specificity and subsequent modification of an amino acid residue through the formation of a covalent bond. There are therefore at least two separate and distinct steps in the process of affinity labeling regardless of whether one is concerned with modification of an enzyme catalytic site or a binding site on a protein not involved in catalysis: the process of specific (selective) binding and the process of covalent bond formation.
Approaches to mitigate the risk of serious adverse reactions in covalent drug design
Published in Expert Opinion on Drug Discovery, 2021
As a medicinal chemistry strategy for the discovery of novel therapeutics and probes for chemical biology, the design of enzyme inhibitors that act by a covalent mechanism has received steadily increasing attention over the past decade, as reflected in the rapid growth of publications on various aspects of the topic dating from around 2009. The term ‘targeted covalent inhibitor’ (TCI) was coined by Singh and colleagues [1] to describe this class of agents, and was defined as follows: ‘An inhibitor bearing a bond-forming functional group of low reactivity that, following binding to the target protein, is positioned to react rapidly with a specific non-catalytic residue at the target site.’ Although an expanded classification of covalent inhibitors has been proposed recently, the term TCI will be used in this article to refer to covalent drugs that operate by the ‘classical affinity label’ mechanism described by Tuley and Fast [2].
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