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A Rigid Helical Peptide Axle for a [2]Rotaxane Molecular Machine

DOI: 10.1002/ange.200904749 DOI Help

Authors: Alessandro Moretto (Universite di Padova) , Ileana Menegazzo (Universite di Padova) , Marco Crisma (Universite di Padova) , Elizabeth Shotton (Diamond Light Source) , Harriott Nowell (Diamond Light Source) , Stefano Mammi (Universite di Padova) , Claudio Toniolo (Universite di Padova)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Angewandte Chemie , VOL 121 (47) , PAGES 9148 - 9151

State: Published (Approved)
Published: November 2009

Abstract: Rotaxanes are mechanically interlocked molecular architec-tures in which a central linear molecule (axle) passes throughthe cavity of a macrocycle (wheel).[1]The axle is held in placeby the presence of sterically bulky stoppers at both ends.Oligomeric systems, which typically consist of repeatingoxyethylene or methylene units, are often exploited as axlesin the construction of rotaxanes.Peptido[2]rotaxanes, based on various -Gly-Xxx- dipep-tide stations in the axle, were first reported by Leigh and co-workers[2]and subsequently by Onagi and Rebek.[3]Morerecently, the Leigh research group described a rotaxane inwhich the wheel is able to protect a bioactive pentapeptideaxle from peptidase-catalyzed hydrolysis.[4]We are currentlyinvestigating the synthesis and properties of a new set ofsymmetrical and nonsymmetrical peptido[2]rotaxanes withamino acid repeating units (oligopeptide systems) in theiraxles. Herein we describe our results on a [2]rotaxane shuttlein which the longest part of the axle is a rigid helical peptide,which was planned to act as a track for the reversible motionof a tetramide macrocyclic wheel.

Journal Keywords: Molecular Devices; Molecular Machines; Rotaxanes; Peptides

Subject Areas: Chemistry


Instruments: I19-Small Molecule Single Crystal Diffraction