title: Stability of crystalline proteins.
abstract: By using two model proteins, glucose oxidase and lipase, we demonstrate that dry crystalline formulations are significantly more stable than their amorphous counterparts. The results of Fourier-transform infrared spectroscopy indicate that crystalline proteins better maintain their native conformation in accelerated stability studies. The lower tendency of crystalline proteins to aggregate is confirmed by size-exclusion chromatography. The data suggest that protein crystallization may significantly improve some aspects of protein handling, and change the way biopharmaceuticals are produced, formulated, and delivered.
authors.affiliation: Altus Biologics, Inc., 625 Putnam Avenue, Cambridge, Massachusetts 02139, USA.
authors.forename: B
authors.initials: B
authors.lastname: Shenoy
authors.forename: Y
authors.initials: Y
authors.lastname: Wang
authors.forename: W
authors.initials: W
authors.lastname: Shan
authors.forename: A L
authors.initials: AL
authors.lastname: Margolin
mesh_terms: D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003460:Crystallization; D005949:Glucose Oxidase / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D005949:Glucose Oxidase