Fast Dynamics Link to Protein Stability in Glasses and Hydrogen-Bond Network Lifetime


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



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.