The acyltransferase function of calreticulin (CRT) was studied using modified coumarin compounds, previously studied 7,8-diacetoxy-4-methylcoumarin (DAMC) and novel 7,8-dipentynoyl-4-methylcoumarin (DPeMC) and 7,8-diazido-4-methylcoumarin (DAzMC). The absorption and fluorescence spectra of all coumarin compounds in ethanol-PBS (1:9 v/v) solution were investigated. The interaction between 7,8-dihydroxy-4-methyl coumarin (DHMC), DAMC, DPeMC, and DAzMC, with CRT were investigated by fluorescence, and FT-IR spectroscopy. The Stern-Volmer quenching constant (K<sub>SV</sub>), the quenching rate constant of the bimolecular reaction (K<sub>q</sub>), the binding constant, and number of binding sites (n) of each coumarin compound with CRT were determined. The CDNB assay was used to determine GST as a receptor protein of the acyl group transferred by CRT. The results were compared to a computational model of ligand- CRT interaction.

Determination of calreticulin-ligand complex formation using fluorescence sprectroscopy

253rd National Meeting (2017)

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