Author: Jitendra Sharma
Mentor: Marcus T. Cicerone
Polymers Division, MSEL
Building 224, Room B118
Mail stop: 8543
Office: (301) 975-4631
Fax: (301) 975-4977
Email: Jitendra@nist.gov
Sigma Xi member: No
Category: Biotechnology
Pharmaceutical industry is increasingly looking for the ways to develop protocols that help stabilize functional proteins in the dry state. Inelastic neutron scattering studies have demonstrated that fast, local dynamics correlates with stability of model proteins in hydrophilic glasses of trehalose and glycerol. We are developing laboratory-scale methods to measure fast, local dynamics in glasses using fluorescence techniques as neutron scattering cannot be used for the routine evaluation of excipients by industry due to limited access to such facilities. We present the fluorescence lifetime and steady state fluorescence data for resorufin in glasses to measure the hydrogen-bonding network lifetime, which is found to be at least in semi-qualitative agreement with the neutron scattering data.