Open Access. Powered by Scholars. Published by Universities.®

Medicine and Health Sciences Commons

Open Access. Powered by Scholars. Published by Universities.®

Chemicals and Drugs

University Faculty Publications and Creative Works

2012

Articles 1 - 2 of 2

Full-Text Articles in Medicine and Health Sciences

Biophysical Characterization Of A Riboflavin-Conjugated Dendrimer Platform For Targeted Drug Delivery, Amanda B. Witte, Christine M. Timmer, Jeremy J. Gam, Seok Ki Choi Feb 2012

Biophysical Characterization Of A Riboflavin-Conjugated Dendrimer Platform For Targeted Drug Delivery, Amanda B. Witte, Christine M. Timmer, Jeremy J. Gam, Seok Ki Choi

University Faculty Publications and Creative Works

The present study describes the biophysical characterization of generation-five poly(amidoamine) (PAMAM) dendrimers conjugated with riboflavin (RF) as a cancer-targeting platform. Two new series of dendrimers were designed, each presenting the riboflavin ligand attached at a different site (isoalloxazine at N-3 and d-ribose at N-10) and at varying ligand valency. Isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC) were used to determine the binding activity for riboflavin binding protein (RfBP) in a cell-free solution. The ITC data shows dendrimer conjugates have K D values of ≥465 nM on a riboflavin basis, an affinity ∼93-fold lower than that of free riboflavin. …


Biophysical Characterization Of A Riboflavin-Conjugated Dendrimer Platform For Targeted Drug Delivery, Amanda B. Witte, Christine M. Timmer, Jeremy J. Gam, Seok Ki Choi Feb 2012

Biophysical Characterization Of A Riboflavin-Conjugated Dendrimer Platform For Targeted Drug Delivery, Amanda B. Witte, Christine M. Timmer, Jeremy J. Gam, Seok Ki Choi

University Faculty Publications and Creative Works

The present study describes the biophysical characterization of generation-five poly(amidoamine) (PAMAM) dendrimers conjugated with riboflavin (RF) as a cancer-targeting platform. Two new series of dendrimers were designed, each presenting the riboflavin ligand attached at a different site (isoalloxazine at N-3 and d-ribose at N-10) and at varying ligand valency. Isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC) were used to determine the binding activity for riboflavin binding protein (RfBP) in a cell-free solution. The ITC data shows dendrimer conjugates have K D values of ≥465 nM on a riboflavin basis, an affinity ∼93-fold lower than that of free riboflavin. …