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Quantifying oligonucleotides binding to human serum albumin with MST: A faster and precise approach for drug candidates ADME profiling

The binding of therapeutic drug candidates to human serum albumin (HSA) and other
plasma proteins needs to be monitored and profiled during the development of drug
candidates as it affects their adsorption, distribution, metabolism, and excretion (ADME).


Antisense oligonucleotides are an emerging therapeutic option to treat diseases with
known genetic origin. The interaction of these oligonucleotides with proteins like HSA
determines their pharmacokinetics (transport and distribution in target tissues) and
pharmacodynamic (binding to the mRNA target) properties and hence their eventual
pharmacology. Fast characterization of their protein-binding properties requires a simple,
robust and reliable method for the quantification of oligonucleotide binding properties to
HSA.


In this work, we illustrate the versatility of MST to determine micromolar binding affinities
of Cy5-labeled oligonucleotides for HSA. Importantly, these Cy5-labeled oligonucleotides
can be used as a tracer to determine the EC50 of an unlabeled oligonucleotide in a
competition assay. 

Previous Video
Measuring multivalent interactions: Uncovering the secrets of virus binding strategies
Measuring multivalent interactions: Uncovering the secrets of virus binding strategies

Up next
Protein labeling – improved quantitation of biomolecular interactions by MST using the His-Tag labeling kit RED-tris-NTA 2nd generation
Protein labeling – improved quantitation of biomolecular interactions by MST using the His-Tag labeling kit RED-tris-NTA 2nd generation

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