Pathway driven self-assembly and living supramolecular polymerization in an amyloid-inspired peptide amphiphile

• Published in: Chemical communications (Cambridge, England) Vol. 54; no. 76; pp. 10730 - 10733
• Main Authors: Singh, Ashmeet, Joseph, Jojo P, Gupta, Deepika, Sarkar, Indranil, Pal, Asish
• Format: Journal Article
• Language: English
• Published: England Royal Society of Chemistry 2018
• Subjects: Amyloidogenic Proteins - chemistry; Dependence; Elastic Modulus; Hydrogels; Hydrogels - chemistry; Nanofibers; Nanofibers - chemistry; Nanoparticles; Nanoparticles - chemistry; Oligopeptides - chemistry; Peptides; Polydispersity; Polymerization; Protein Conformation, beta-Strand; Protein Multimerization; Seeds; Self-assembly; Surface-Active Agents - chemistry; Temperature
• ISSN: 1359-7345; 1364-548X
• DOI: 10.1039/c8cc06266h

Peptide 1 with an Aβ42 amyloid nucleating core demonstrates step-wise self-assembly in water. Variation of temperature or solvent composition arrests the self-assembly to give metastable nanoparticles, which undergo self-assembly on gradual increase in temperature and eventually produce kinetically controlled nanofibers and thermodynamically stable twisted helical bundles. Mechanical agitation of the fibers provided access to short seeds with narrow polydispersity index, which by mediation of seeded supramolecular polymerization establishes perfect control over the length of the nanofibers. Such pathway dependence and the length control of the supramolecular peptide nanofibers is exploited to tune the mechanical strength of the resulting hydrogel materials.