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...

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Veröffentlicht in:Chemistry, an Asian journal an Asian journal, 2011-02, Vol.6 (2), p.452-458
Hauptverfasser: Park, Il-Soo, Yoon, You-Rim, Jung, Minseon, Kim, Kimoon, Park, SeongByeong, Shin, Seokmin, Lim, Yong-beom, Lee, Myongsoo
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Sprache:eng
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Zusammenfassung: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. Lock, stock, and β barrel: β‐Barrel protein mimics of dual functionality have been developed through the self‐assembly of β‐sheet‐forming peptides (see graphic). A unique feature of this system is the formation of highly uniform and discrete water‐soluble β‐barrel nanoring structures highly similar to natural β‐barrel proteins in structure and composition.
ISSN:1861-4728
1861-471X
DOI:10.1002/asia.201000428