|
KMID : 1094720110160030477
|
|
Biotechnology and Bioprocess Engineering
2011 Volume.16 No. 3 p.477 ~ p.481
|
|
|
Optimization of expression, purification, and NMR measurement for structural studies of transmembrane region of amyloid β protein
|
|
Park Tae-Joon
Kim Ji-Sun
Choi Sung-Sub
Kim Yong-Ae
|
|
|
Abstract
|
|
|
|
The amyloid precursor protein (APP) is an integral transmembrane protein which has been suggested to play a central role in the pathogenesis of Alzheimer’s disease. Despite the enormous amount of research conducted on amyloid protein, the precise mechanism of its toxic effect is not yet fully understood. To better understand the mechanism and function of amyloid protein, it is critical to elucidate the three-dimensional structure of the single transmembrane spanning region of human APP (hAPP-TM). Unfortunately, it is difficult to prepare the peptide sample because hAPP-TM is a membrane-bound protein that transverses the lipid bilayer of the cell membrane. Generally, the preparation of a transmembrane peptide is very difficult and time-consuming. In fact, high yield production of transmembrane peptides has been limited by experimental difficulties related to insufficient yields and the low solubility of such peptides. In this study, we describe experimental processes developed to optimize the expression, purification, and NMR measurement conditions for hAPP-TM transmembrane peptide.
|
|
|
KEYWORD
|
|
|
amyloid, transmembrane protein, HPLC, purification, NMR
|
|
|
FullTexts / Linksout information
|
|
|
|
|
Listed journal information
|
|
 
|
|