Stacking interactions by two Phe side chains stabilize and orient assemblies of even the minimal amphiphilic β-sheet motif

Zarzhitsky Shlomo; T. P. Vinod; Raz Jelinek; Hanna Rapaport

doi:10.1039/c4cc09673h

Stacking interactions by two Phe side chains stabilize and orient assemblies of even the minimal amphiphilic β-sheet motif

Zarzhitsky Shlomo, T. P. Vinod, Raz Jelinek, Hanna Rapaport

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

Here we demonstrate that the smallest possible motif of the amphiphilic and pleated β-strand structure can be generated using tri-peptides stabilized by π-π stacking interactions. Monitoring the early stages of Phe-Glu-Phe fibril formation revealed unique angular orientations. Phe-Glu-Phe fibrils were further exploited as adsorbing templates for metal ions.

Original language	English
Pages (from-to)	3154-3157
Number of pages	4
Journal	Chemical Communications
Volume	51
Issue number	15
DOIs	https://doi.org/10.1039/c4cc09673h
State	Published - 21 Feb 2015

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry (all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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abstract = "Here we demonstrate that the smallest possible motif of the amphiphilic and pleated β-strand structure can be generated using tri-peptides stabilized by π-π stacking interactions. Monitoring the early stages of Phe-Glu-Phe fibril formation revealed unique angular orientations. Phe-Glu-Phe fibrils were further exploited as adsorbing templates for metal ions.",

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AU - Shlomo, Zarzhitsky

AU - Vinod, T. P.

AU - Jelinek, Raz

AU - Rapaport, Hanna

N1 - Publisher Copyright: © The Royal Society of Chemistry 2015.

PY - 2015/2/21

Y1 - 2015/2/21

N2 - Here we demonstrate that the smallest possible motif of the amphiphilic and pleated β-strand structure can be generated using tri-peptides stabilized by π-π stacking interactions. Monitoring the early stages of Phe-Glu-Phe fibril formation revealed unique angular orientations. Phe-Glu-Phe fibrils were further exploited as adsorbing templates for metal ions.

AB - Here we demonstrate that the smallest possible motif of the amphiphilic and pleated β-strand structure can be generated using tri-peptides stabilized by π-π stacking interactions. Monitoring the early stages of Phe-Glu-Phe fibril formation revealed unique angular orientations. Phe-Glu-Phe fibrils were further exploited as adsorbing templates for metal ions.

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AN - SCOPUS:84929999970

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Stacking interactions by two Phe side chains stabilize and orient assemblies of even the minimal amphiphilic β-sheet motif

Abstract

ASJC Scopus subject areas

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