Multiplexing natural orientation: oppositely directed self-assembling peptides
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Updated: Apr 30, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Woo-Jin Jeong1, Sanghun Han, Hyeseo Park
1Translational Research Center for Protein Function Control and Department of Materials Science & Engineering, Yonsei University , Seoul 120-749, Korea.
Abstract:
We explore here the possibility that polypeptide chains with directional multiplicity might provide for the control of peptide self-assembly processes. We tested this new possibility using an oppositely directed peptide (ODP) supramolecular system. The ODP could make it possible to form a βαβ motif with antiparallel β-sheets, which does not exist in nature. Furthermore, the designed ODPs were able to self-assemble into discrete, homogeneous, and structured protein-like controlled nano-objects. ODPs represent a simple but powerful unnatural self-assembling peptide system that can become a basic scaffold for fabricating more complex and elaborate artificial nanostructures.
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