Effects of propyl gallate on interaction between TNF-alpha and sTNFR-I using an affinity biosensor
Abstract
Aim: To study the effects of propyl gallate on the interaction of tumor necrosis factor-alpha (TNF-alpha) with its soluble receptor, sTNFR-I.
Methods: Interactions between TNF-alpha and sTNFR-I were analyzed using an IAsys biosensor. sTNFR-I was immobilized on the carboxymethyl dextran (CMD) surface of the IAsys biosensor cuvettes, and TNF-alpha preincubated with different concentrations of propyl gallate was added to the cuvettes. The resonant angle shift caused by the binding between TNF-alpha and sTNFR-I was then recorded.
Results: sTNFR-I was immobilized on the CMD surface at a density of 2.76 ng/mm2. TNF-alpha then bound the immobilized sTNFR-I specifically, and propyl gallate was able to enhance the binding between TNF-alpha and sTNFR-I in a dose-dependent manner.
Conclusion: The binding between TNF-alpha and sTNFR-I is one of the targets that propyl gallate can act on in vivo. The IAsys biosensor offers a new clue as to the study on the mechanisms of action of propyl gallate.
Keywords:
Methods: Interactions between TNF-alpha and sTNFR-I were analyzed using an IAsys biosensor. sTNFR-I was immobilized on the carboxymethyl dextran (CMD) surface of the IAsys biosensor cuvettes, and TNF-alpha preincubated with different concentrations of propyl gallate was added to the cuvettes. The resonant angle shift caused by the binding between TNF-alpha and sTNFR-I was then recorded.
Results: sTNFR-I was immobilized on the CMD surface at a density of 2.76 ng/mm2. TNF-alpha then bound the immobilized sTNFR-I specifically, and propyl gallate was able to enhance the binding between TNF-alpha and sTNFR-I in a dose-dependent manner.
Conclusion: The binding between TNF-alpha and sTNFR-I is one of the targets that propyl gallate can act on in vivo. The IAsys biosensor offers a new clue as to the study on the mechanisms of action of propyl gallate.