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Designer Nanorings with Functional Cavities from Self‐Assembling β‐Sheet Peptides
Author(s) -
Park IlSoo,
Yoon YouRim,
Jung Minseon,
Kim Kimoon,
Park SeongByeong,
Shin Seokmin,
Lim Yongbeom,
Lee Myongsoo
Publication year - 2011
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.201000428
Subject(s) - barrel (horology) , transmembrane protein , nanoreactor , supramolecular chemistry , nanotechnology , self assembly , folding (dsp implementation) , chemistry , biophysics , molecule , materials science , biochemistry , biology , engineering , receptor , organic chemistry , nanoparticle , electrical engineering , composite material
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.