Self-Assembling Peptide Surfactants A6K and A6D Adopt α-Helical Structures Useful for Membrane Protein Stabilization

Membranes

Furen Zhuang¹  Kamila Oglᆜka¹ 

[1] Institute of Bioengineering and Nanotechnology, 31 Biopolis Way, The Nanos #04–01, Singapore 138669;

关键词: self-assembling peptides;    membrane proteins;    peptide surfactants;    peptide structure;    GPCRs;   

DOI  :  10.3390/membranes1040314

来源: mdpi

【 摘 要 】

Elucidation of membrane protein structures have been greatly hampered by difficulties in producing adequately large quantities of the functional protein and stabilizing them. A₆D and A₆K are promising solutions to the problem and have recently been used for the rapid production of membrane-bound G protein-coupled receptors (GPCRs). We propose that despite their short lengths, these peptides can adopt α-helical structures through interactions with micelles formed by the peptides themselves. These α-helices are then able to stabilize α-helical motifs which many membrane proteins contain. We also show that A₆D and A₆K can form β-sheets and appear as weak hydrogels at sufficiently high concentrations. Furthermore, A₆D and A₆K together in sodium dodecyl sulfate (SDS) can form expected β-sheet structures via a surprising α-helical intermediate.

【 授权许可】

CC BY   
© 2011 by the authors; licensee MDPI, Basel, Switzerland.