Designed Amphiphilic β‑Sheet Peptides as Templates for Paraoxon Adsorption and Detection

Amphiphilic peptides were designed to fold into a β-sheet monolayer structure while presenting the catalytic triad residues of the enzyme, acetylcholinesterase (Glu, His, and Ser), to a solution containing the organophosphate, paraoxon. Three peptides, in which the catalytic triad residues were arra...

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Veröffentlicht in:Langmuir 2013-06, Vol.29 (23), p.6840-6848
Hauptverfasser: Yaakobi, Keren, Liebes-Peer, Yael, Kushmaro, Ariel, Rapaport, Hanna
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container_end_page 6848
container_issue 23
container_start_page 6840
container_title Langmuir
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creator Yaakobi, Keren
Liebes-Peer, Yael
Kushmaro, Ariel
Rapaport, Hanna
description Amphiphilic peptides were designed to fold into a β-sheet monolayer structure while presenting the catalytic triad residues of the enzyme, acetylcholinesterase (Glu, His, and Ser), to a solution containing the organophosphate, paraoxon. Three peptides, in which the catalytic triad residues were arranged in different orders along the strand, were generated to reveal potential differences in interactions with paraoxon as a function of the order of these amino acids. One additional peptide with amino acids introduced in random order was studied to highlight the contribution of the β-sheet secondary structure to any interactions with paraoxon. Langmuir isotherms, Brewster angle microscope at interfaces, and circular dichroism measurements in bulk showed that both the β-sheet conformation and the order of the amino acids along the strand influenced the interactions of paraoxon with the peptides. Compression isotherm curves as well as Brewster angle microscopy images provided evidence for enhanced adsorption of the paraoxon to the monolayers of peptides, which present neighboring Glu and Ser residues along the hydrophilic face of the β-strand. Circular dichroism revealed that the peptide most sensitive to interactions with paraoxon was that with the triad residues in the order Glu, Ser, and His, which appears to be appropriate for supporting a catalytic mechanism similar to that in the acetylcholinesterase enzyme. These rationally designed peptides may be further used for the development of technologies for organophosphate adsorption and detection.
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Three peptides, in which the catalytic triad residues were arranged in different orders along the strand, were generated to reveal potential differences in interactions with paraoxon as a function of the order of these amino acids. One additional peptide with amino acids introduced in random order was studied to highlight the contribution of the β-sheet secondary structure to any interactions with paraoxon. Langmuir isotherms, Brewster angle microscope at interfaces, and circular dichroism measurements in bulk showed that both the β-sheet conformation and the order of the amino acids along the strand influenced the interactions of paraoxon with the peptides. Compression isotherm curves as well as Brewster angle microscopy images provided evidence for enhanced adsorption of the paraoxon to the monolayers of peptides, which present neighboring Glu and Ser residues along the hydrophilic face of the β-strand. 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subjects Adsorption
Chemistry
Exact sciences and technology
General and physical chemistry
Models, Molecular
Paraoxon - chemistry
Particle Size
Peptides - chemical synthesis
Peptides - chemistry
Surface physical chemistry
Surface Properties
Surface-Active Agents - chemical synthesis
Surface-Active Agents - chemistry
title Designed Amphiphilic β‑Sheet Peptides as Templates for Paraoxon Adsorption and Detection
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