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.
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.