Designer nanorings with functional cavities from self-assembling β-sheet peptides.
β-Barrel proteins that take the shape of a ring are common in many types of water-soluble enzymes and water-insoluble transmembrane pore-forming proteins. Since β-barrel proteins perform diverse functions in the cell, it would be a great step towards developing artificial proteins if we can control the polarity of artificial β-barrel proteins at will. Here, we describe a rational approach to construct β-barrel protein mimics from the self-assembly of peptide-based building blocks. With this approach, the direction of the self-assembly process toward the formation of water-soluble β-barrel nanorings or water-insoluble transmembrane β-barrel pores could be controlled by the simple but versatile molecular manipulation of supramolecular building blocks. This study not only delineates the basic driving force that underlies the folding of β-barrel proteins, but also lays the foundation for the facile fabrication of β-barrel protein mimics, which can be developed as nanoreactors, ion- and small-molecule-selective pores, and novel antibiotics.
Park
Il-Soo
IS
Center for Supramolecular Nano-Assembly and Department of Chemistry, Seoul National University, Seoul 151-747, Korea.
Yoon
You-Rim
YR
Jung
Minseon
M
Kim
Kimoon
K
Park
SeongByeong
S
Shin
Seokmin
S
Lim
Yong-beom
YB
Lee
Myongsoo
M
D040761:Biomimetic Materials / Q000138:chemical synthesis / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
D008051:Lipid Bilayers; D010455:Peptides