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Related Experiment Video

Updated: Jun 27, 2026

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

Nucleobase-directed amyloid nanotube assembly.

Peng Liu¹, Rong Ni, Anil K Mehta

¹Center for Fundamental and Applied Molecular Evolution, Department of Chemistry, Emory University, Atlanta, Georgia 30322, USA.

Journal of the American Chemical Society

|December 5, 2008

Summary

Researchers created novel nanotubes by incorporating cytosine nucleobases into amyloid peptides. These self-assembling ccAQLVFFA structures exhibit a beta-sheet-rich architecture, forming well-defined nanotubes via complementary base interactions.

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DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers

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Published on: October 25, 2017

Area of Science:

Biomaterials Science
Supramolecular Chemistry
Nanotechnology

Background:

Amyloid peptides are known for self-assembly into beta-sheet structures.
Nucleobase incorporation into peptides offers new functional possibilities.
Controlled self-assembly is key for designing advanced nanomaterials.

Purpose of the Study:

To synthesize and characterize a novel nucleobase-peptide conjugate (ccAQLVFFA).
To investigate the self-assembly behavior of ccAQLVFFA into higher-order structures.
To explore the role of cytosine complementarity in directing nanotube formation.

Main Methods:

Peptide synthesis incorporating cytosine nucleobases.
Small-angle X-ray scattering (SAXS) for structural analysis.
Fourier-transform infrared spectroscopy (FT-IR) and X-ray diffraction (XRD) for assembly confirmation.
Solid-state Nuclear Magnetic Resonance (NMR) and linear dichroism for beta-sheet registry determination.

Main Results:

Successful incorporation of cytosine into the amyloid peptide fragment HHQALVFFA, yielding ccAQLVFFA.
Formation of well-defined nanotubes (24.8 nm outer diameter, 3.3 nm wall thickness) at pH 3-4.
Confirmation of beta-sheet-rich assembly with cross-beta architecture.
Cytosine bases positioned perpendicular to the nanotube axis, enhancing beta-sheet stacking through complementary interactions.

Conclusions:

Cytosine-functionalized amyloid peptides can self-assemble into ordered nanotubes.
Complementary interactions of nucleobases within the peptide side chains drive the formation of nanotube architecture.
This work expands the concept of information encoding beyond nucleic acid duplexes into self-assembling covalent networks.