https://pubs.acs.org/doi/10.1021/cen-10311-cover
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Modalities
Here are some of the modalities that medicinal chemists can choose among when they set out to interrupt the function of a disease-related protein or other biomolecule.
Competitive inhibitors: Mimic a substrate and occupy the active site of an enzyme
Allosteric modulators: Bind somewhere other than the active site to influence an enzyme’s action
Covalent inhibitors: Covalently bind to a target protein, and change its conformation to block activity
PROTACs and other bifunctional molecules: Bind to two different proteins to drive outcomes such as protein degradation
Molecular glues:Stabilize the interface between two proteins—often aiming to degrade one of the two
Splice modifiers: Change the alternative splicing of an RNA molecule, affecting how the related protein is made
Monoclonal antibodies: Bind to targets on the cell surface with high specificity Bispecific antibodies: Modified to bind to two different targets Antibody-drug conjugates: Deliver drugs (usually chemotherapies) to cells specified by an antibody
Antibody fragments and light-chain antibodies: Bind to specific epitopes, but are smaller than a monoclonal antibody
Peptides: Usually bind to receptors, mimicking hormones
Cyclic peptides: Act as linear peptides do, but with smaller 3D structure, offering large-molecule specificity but lower degradation CRISPR and related technologies: Alter DNA encoding disease-related proteins Interfering RNA and antisense oligonucleotides: Block production of proteins from RNA
RNA aptamers: Bind to target molecules, sometimes used to block or activate signaling
mRNA: Introduces desired proteins to be made
RNA editors:Alter a target RNA by one or a few bases to change protein sequence Cell therapies: Bind to and kill specific cells, usually recognizing cancer epitopes
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