Chemical biology
A glutathione probe finds caffeine as a CaSR PAM
Open access · cc by · source: Europe PMC
Photoaffinity GSH analog DAZ-G labels the CaSR amino-acid site and shows caffeine is a positive allosteric modulator.
Key findings
DAZ-G binds the amino-acid binding site and is a potent PAM. Caffeine at 0–1 μM enhances labeling via the calcium-binding site, while higher concentrations compete at the amino-acid site; caffeine raises Ca2+ only when extracellular Ca2+ is present.
Methodology
Authors synthesized DAZ-G (diazirine/alkyne GSH), photocrosslinked it to CaSR in HEK293 cells, competed with known ligands, and read intracellular Ca2+ flux to test whether caffeine activates the receptor.
Limitations
The probe is currently a Western-blot tool, not a high-throughput screen, and caffeine’s in vivo CaSR contribution versus adenosine receptors is not measured here.
How this study connects
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Photoaffinity GSH analog DAZ-G labels the CaSR amino-acid site and shows caffeine is a positive allosteric modulator.
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