BIOPHYSICAL EVALUATION OF SOL-GEL ENCAPSULATED PROTEINS

Project: Research project

Project Details

Description

DESCRIPTION: (applicant's abstract) The encapsulation of proteins in porous
sol-gels has captured the attention of both applied and basic research
scientists because the encapsulated proteins retain functional activity and
exhibit enhanced stability. Despite the widespread interest in using this
technology to develop new classes of robust biosensors, no in-depth biophysical
study of protein response to sol-gel encapsulation has been carried out. The
project proposed herein will systematically examine the impact of three
promising encapsulation protocols on the conformation and dynamics of the
well-characterized heme proteins, hemoglobin and myoglobin. We have probed the
solution-phase conformation - secondary through quaternary - of these heme
proteins with a myriad of laser-based time-resolved and steady state
spectroscopic techniques, and are therefore uniquely qualified to examine the
dynamic and static heme protein/sol-gel interactions. The spectroscopic tools
at our fingertips include: CW UV resonance Raman, CW and time-resolved visible
resonance Raman, time-resolved near IR absorption, time resolved fluorescence
anisotropy and fluorescence lifetime measurements. Subtle as well as
large-scale conformational changes and the associated dynamics are probed when
combining these techniques. In addition, nanosecond, time-resolved absorption
spectroscopy will primarily be used to characterize the ligand rebinding
kinetics of the heme proteins in the sol-gels. It is anticipated that this
comprehensive study will result in an algorithm for matching an encapsulation
protocol to a particular biomedical or biophysical application.
StatusFinished
Effective start/end date3/1/002/28/02

Funding

  • National Heart, Lung, and Blood Institute: $333,778.00
  • National Heart, Lung, and Blood Institute: $324,507.00

ASJC

  • Biophysics
  • Spectroscopy

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