Stability of crystalline proteins

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 conformati...

Full description

Saved in:
Bibliographic Details
Published in:Biotechnology and bioengineering 2001-06, Vol.73 (5), p.358-369
Main Authors: Shenoy, Bhami, Wang, Yi, Shan, Weizhong, Margolin, Alexey L.
Format: Article
Language:English
Subjects:
Biological and medical sciences
Biotechnology
Chromatography, Gel
Chromatography, High Pressure Liquid
crystalline proteins
Crystallization
drug formulation
Fundamental and applied biological sciences. Psychology
Glucose Oxidase - chemistry
Health. Pharmaceutical industry
Industrial applications and implications. Economical aspects
Miscellaneous
protein crystals
protein stability
Protein Structure, Secondary
Spectroscopy, Fourier Transform Infrared
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 73: 358–369, 2001.
ISSN:0006-3592
1097-0290
DOI:10.1002/bit.1069