Event Title

P-31 Preliminary Study of the Effect of PAMAM Dendrimers on Mushroom Tyrosinase Activity

Presenter Information

Andrew Hong, Andrews University

Location

Buller Hallway

Start Date

3-6-2015 2:30 PM

End Date

3-6-2015 4:00 PM

Description

Traditional polymer chemistry has focused widely on the use of linear polymers; however, the unique properties of highly branched polymers, called dendrimers, exhibit different functional uses as opposed to their linear counterparts. A well characterized enzyme, mushroom tyrosinase, was chosen to investigate the biological function changes, if any, by dendrimers. Our study first evaluated the kinetics of mushroom tyrosinase, then observed and tested its function in the presence of PAMAMs (polyamidodiamines) dendrimers. Tyrosinase assays showed distinct inhibition as the concentration of the dendrimer (PAMAM G1) increased from 0.2 mM to 5 mM. From the analysis of the Lineweaver-Burk plots, the dendrimer had a mixed inhibitory effect on the enzyme, in which it is binding to the enzyme and to the enzyme-substrate complex to inhibit both species simultaneously. Mushroom tyrosinase and dendrimer interactions can be extensively studied as models for other enzymes and allow for further study of the biological applications of dendrimers.

Acknowledgments

Advisor: D. David Nowack, Chemistry & Biochemistry

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Mar 6th, 2:30 PM Mar 6th, 4:00 PM

P-31 Preliminary Study of the Effect of PAMAM Dendrimers on Mushroom Tyrosinase Activity

Buller Hallway

Traditional polymer chemistry has focused widely on the use of linear polymers; however, the unique properties of highly branched polymers, called dendrimers, exhibit different functional uses as opposed to their linear counterparts. A well characterized enzyme, mushroom tyrosinase, was chosen to investigate the biological function changes, if any, by dendrimers. Our study first evaluated the kinetics of mushroom tyrosinase, then observed and tested its function in the presence of PAMAMs (polyamidodiamines) dendrimers. Tyrosinase assays showed distinct inhibition as the concentration of the dendrimer (PAMAM G1) increased from 0.2 mM to 5 mM. From the analysis of the Lineweaver-Burk plots, the dendrimer had a mixed inhibitory effect on the enzyme, in which it is binding to the enzyme and to the enzyme-substrate complex to inhibit both species simultaneously. Mushroom tyrosinase and dendrimer interactions can be extensively studied as models for other enzymes and allow for further study of the biological applications of dendrimers.