Designer short peptide surfactants stabilize G protein-coupled receptor bovine rhodopsin

Designer short peptide surfactants stabilize G protein-coupled receptor bovine rhodopsin
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DOI:
10.1073/pnas.0607167103
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发表时间:
2006-11
期刊:
Proceedings of the National Academy of Sciences
影响因子:
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通讯作者:
Xiaojun Zhao;Y. Nagai;P. Reeves;Patrick J. Kiley;H. Khorana;Shuguang Zhang
Xiaojun Zhao;Y. Nagai;P. Reeves;Patrick J. Kiley;H. Khorana;Shuguang Zhang
中科院分区:
其他
文献类型:
--
作者:
Xiaojun Zhao;Y. Nagai;P. Reeves;Patrick J. Kiley;H. Khorana;Shuguang Zhang

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Membrane proteins play vital roles in every aspect of cellular activities. To study diverse membrane proteins, it is crucial to select the right surfactants to stabilize them for analysis. Despite much effort, little progress has been made in elucidating their structure and function, largely because of a lack of suitable surfactants. Here we report the stabilization of a G protein-coupled receptor bovine rhodopsin in solution, using a new class of designer short and simple peptide surfactants. These surfactants consist of seven amino acids with a hydrophilic head, aspartic acid or lysine, and a hydrophobic tail with six consecutive alanines. These peptide surfactants not only enhance the stability of bovine rhodopsin in the presence of lipids and the common surfactants n-dodecyl-β-d-maltoside and octyl-d-glucoside, but they also significantly stabilize rhodopsin under thermal denaturation conditions, even after lipids are removed. These peptide surfactants are simple, versatile, effective, and affordable. They represent a designer molecular nanomaterial for use in studies of diverse elusive membrane proteins.