(2009) Towards a microarray of functional membrane proteins: Assembly of a surface-attachable, membrane-protein-anchored membrane structure using apolipoprotein A-1
Towards a microarray of functional membrane proteins: Assembly of a surface-attachable, membrane-protein-anchored membrane structure using apolipoprotein A-1.
Kyungwon Lee, Jae-Yoon Shin, Yoo-Soo Yang, Jae-Il Shin, Yong-Cheol Park, Jin-Ho Seo, Tai-Hyun Park, Chol-Su Shin, Yong-Su Jin and Dae-Hyuk Kweon*
Enzyme and Microbial Technology 44(2): 217-222 2009.04.06.
(SCI I/F: 2.367)
ApolipoproteinA-1 (apoA-I) forms a discoidal membranestructure with phospholipids during the formation of high density lipoprotein and plays a role in the reverse cholesterol transport pathway. The discoidal membrane nanostructure, Nanodisc, can be easily assembled in vitro using apoA-I protein and phospholipids. In this study, the possibility of exploiting this unique membranestructure for the immobilization of membraneproteins on solid surfaces while the proteins are embedded in the membrane was investigated. By using His6-tagged full-length apoA-I, asurface-attachable, membrane-protein-anchoredmembrane (SAMPAM) structure, in which membraneproteins of interest are embedded into the membrane, was reconstituted. When the SAMPAM was immobilized on a Ni-NTA surface, the structure maintained its size and shape, indicating that the new proposed architecture may be useful for the display of membraneproteins on a solid surface in amembrane-associated form.
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