Self-assembly of phenylalanine oligopeptides: Insights from experiments and simulations

Phanourios Tamamis, Lihi Adler-Abramovich, Meital Reches, Karen Marshall, Pawel Sikorski, Louise Serpell, Ehud Gazit*, Georgios Archontis

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

208 Scopus citations

Abstract

Studies of peptide-based nanostructures provide general insights into biomolecular self-assembly and can lead material engineering toward technological applications. The diphenylalanine peptide (FF) self-assembles into discrete, hollow, well ordered nanotubes, and its derivatives form nanoassemblies of various morphologies. Here we demonstrate for the first time, to our knowledge, the formation of planar nanostructures with β-sheet content by the triphenylalanine peptide (FFF). We characterize these structures using various microscopy and spectroscopy techniques. We also obtain insights into the interactions and structural properties of the FF and FFF nanostructures by 0.4-μs, implicit-solvent, replica-exchange, molecular-dynamics simulations of aqueous FF and FFF solutions. In the simulations the peptides form aggregates, which often contain open or ring-like peptide networks, as well as elementary and network-containing structures with β-sheet characteristics. The networks are stabilized by polar and nonpolar interactions, and by the surrounding aggregate. In particular, the charged termini of neighbor peptides are involved in hydrogen-bonding interactions and their aromatic side chains form "T-shaped" contacts, as in three-dimensional FF crystals. These interactions may assist the FF and FFF self-assembly at the early stage, and may also stabilize the mature nanostructures. The FFF peptides have higher network propensities and increased aggregate stabilities with respect to FF, which can be interpreted energetically.

Original languageAmerican English
Pages (from-to)5020-5029
Number of pages10
JournalBiophysical Journal
Volume96
Issue number12
DOIs
StatePublished - 2009
Externally publishedYes

Bibliographical note

Funding Information:
This work was funded by a grant from the A. G. Leventis Foundation (to G.A. and Ph.T). L.A.A. gratefully acknowledges the support of the Colton Foundation.

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