Protein-based drug formulation in solid and solution states-changes in protein secondary structure analyzed by FT-IR spectroscopy

BIOL 162

Shuowei Cai, scai@umassd.edu, Department of Chemistry and Biochemistry, University of Massachusetts Dartmouth, North Dartmouth, MA 02747
Fourier transform infrared spectroscopy is increasingly becoming an important method to determine secondary structure of peptides and proteins. FTIR is not only useful for solution state, but also applicable to solid samples. In this study, we compared the protein structures in solid and aqueous solution states. We have observed that for most ?-helix dominant proteins, the ?-type structures significantly increased in their solid state, this increase in ?-structure is reversible when they are rehydrated in solution. ?-sheet dominant proteins, on the other hand, have similar structures between solid and solution state. This research has significant impact on pharmaceutical industry, since many protein based therapeutics need to be formulated into solid state, and their structural information need to be investigated in order to keep their structure as intact as in aqueous solution in the physiological conditions. The research was in part supported by Amgen Corp.

 

Frontiers in Chemical Biology
5:00 PM-7:00 PM, Wednesday, August 22, 2007 BCEC -- Exhibit Hall - B2, Poster

Division of Biological Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007