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Self-assembling Peptide Detergent A6D Directly Associates with Bovine Rhodopsin and Forms Lipid-like Vesicles

Published online by Cambridge University Press:  01 February 2011

Xiaojun Zhao ,
Yusuke Nagai  and
Shuguang Zhang
Xiaojun Zhao
Affiliation:
Center for Biomedical Engineering NE47-379, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USA Both authors are contributed equally
Yusuke Nagai
Affiliation:
Center for Biomedical Engineering NE47-379, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USA Both authors are contributed equally
Shuguang Zhang*
Affiliation:
Center for Biomedical Engineering NE47-379, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USA Center for Bits & Atoms Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USA
*
*Shuguang@mit.edu, http://web.mit.edu/lms/www/ Tel: 617-258-7514, FAX: 617-258-5239
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Abstract

Membrane protein study critically depends on detergents, which are amphilhilic molecules containing a hydrophilic “head” and a hydrophobic “tail” to mimic biological lipid bilayers to stabilize membrane proteins. However, detergents are not fully equivalent to lipid bilayers and in fact they only partly mimic lipid bilayers function. Consequently, membrane proteins in detergent solution are more or less denatured because detergents can not effectively stabilize membrane protein structures. Therefore, it is urgent to develop new types of detergents for more effectively stabilizing membrane proteins. Previously, we have reported a new type of self-assembly peptide detergents containing a hydrophilic head composed of either a negatively charged aspartic acid or a positively charged lysine and a tail of hydrophobic amino acids of six connective alanines. This new peptide detergent has been shown to be more effective for protecting membrane protein PS I structure than that the conventional detergent does. However, what type of physical structures peptide detergent can form is unclear yet. Here we presented our AFM and DSL analysis of the peptide detergent A6D, which not only form mixed micelles with n-Octyl-beta-D-Glucoside (OG) to solubilize membrane protein rhodopsin, but also can mimic lipid bilayers to keep rhodopsin in lipid-like vesicles for its structure preservation.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 845: Symposium AA – Nanoscale Materials Science in Biology and Medicine , 2004 , AA5.51
Copyright
Copyright © Materials Research Society 2005

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References

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