Poly(l‑proline)-Stabilized Polypeptide Nanostructures via Ring-Opening Polymerization-Induced Self-Assembly (ROPISA)

Poly­(proline) II helical motifs located at the protein–water interface stabilize the three-dimensional structures of natural proteins. Reported here is the first example of synthetic biomimetic poly­(proline)-stabilized polypeptide nanostructures obtained by a straightforward ring-opening polymeriz...

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Bibliographic Details
Published inACS macro letters Vol. 13; no. 8; pp. 1031 - 1036
Main Authors Tinajero-Díaz, Ernesto, Judge, Nicola, Li, Bo, Leigh, Thomas, Murphy, Robert D., Topham, Paul D., Derry, Matthew J., Heise, Andreas
Format Journal Article
LanguageEnglish
Published American Chemical Society 20.08.2024
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Summary:Poly­(proline) II helical motifs located at the protein–water interface stabilize the three-dimensional structures of natural proteins. Reported here is the first example of synthetic biomimetic poly­(proline)-stabilized polypeptide nanostructures obtained by a straightforward ring-opening polymerization-induced self-assembly (ROPISA) process through consecutive N-carboxyanhydride (NCA) polymerization. It was found that the use of multifunctional 8-arm initiators is critical for the formation of nanoparticles. Worm-like micelles as well as spherical morphologies were obtained as confirmed by dynamic light scattering (DLS), transmission electron microscopy (TEM), and small angle X-ray scattering (SAXS). The loading of the nanostructures with dyes is demonstrated. This fast and open-vessel procedure gives access to amino acids-based nanomaterials with potential for applications in nanomedicine.
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ISSN:2161-1653
2161-1653
DOI:10.1021/acsmacrolett.4c00400