Cooperative self-assembly of peptide gelators and proteins

Nadeem Javid, Sangita Roy, Mischa Zelzer, Zhimou Yang, Jan Sefcik, Rein V. Ulijn

Research output: Contribution to journalArticlepeer-review

59 Citations (Scopus)
184 Downloads (Pure)

Abstract

Molecular self-assembly provides a versatile route for the production of nanoscale materials for medical and technological applications. Herein, we demonstrate that the cooperative self-assembly of amphiphilic small molecules and proteins can have drastic effects on supramolecular nanostructuring of resulting materials. We report that mesoscale, fractal-like clusters of proteins form at concentrations that are orders of magnitude lower compared to those usually associated with molecular crowding at room temperature. These protein clusters have pronounced effects on the molecular self-assembly of aromatic peptide amphiphiles (fluorenylmethoxycarbonyl- dipeptides), resulting in a reversal of chiral organization and enhanced order through templating and binding. Moreover, the morphological and mechanical properties of the resultant nanostructured gels can be controlled by the cooperative self-assembly of peptides and protein fractal clusters, having implications for biomedical applications where proteins and peptides are both present. In addition, fundamental insights into cooperative interplay of molecular interactions and confinement by clusters of chiral macromolecules is relevant to gaining understanding of the molecular mechanisms of relevance to the origin of life and development of synthetic mimics of living systems.

Original languageEnglish
Pages (from-to)4368–4376
Number of pages9
JournalBiomacromolecules
Volume14
Issue number12
Early online date20 Nov 2013
DOIs
Publication statusPublished - 9 Dec 2013

Keywords

  • cooperative self assembly
  • biomaterials
  • hydrogel
  • chiral inversion
  • supramolecular chirality
  • protein fractals
  • peptide gelators

Fingerprint

Dive into the research topics of 'Cooperative self-assembly of peptide gelators and proteins'. Together they form a unique fingerprint.

Cite this