Presentation Title

P-28 Preliminary Study of the Effect of PAMAM Dendrimers on Mushroom Tyrosinase Activity

Presenter Status

Undergraduate Student, Department of Chemistry and Biochemistry

Second Presenter Status

Department of Chemistry and Biochemistry

Preferred Session

Poster Session

Location

Buller Hallway

Start Date

31-10-2014 1:30 PM

End Date

31-10-2014 3:00 PM

Presentation Abstract

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, caused by dendrimers. Our study measured the kinetic’s parameters (KM and Vmax) of mushroom tyrosinase, then observed those parameters in the presence of PAMAMs (polyamidodiamines) dendrimers. Tyrosinase assays showed distinct inhibition of KM and Vmax 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.

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Oct 31st, 1:30 PM Oct 31st, 3:00 PM

P-28 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, caused by dendrimers. Our study measured the kinetic’s parameters (KM and Vmax) of mushroom tyrosinase, then observed those parameters in the presence of PAMAMs (polyamidodiamines) dendrimers. Tyrosinase assays showed distinct inhibition of KM and Vmax 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.