Folding-and-Assembly Strategy

  • ChemPubSoc Europe Logo
  • Author: Andrei Dragan
  • Published Date: 14 May 2017
  • Source / Publisher: Chemistry – An Asian Journal/Wiley-VCH
  • Copyright: Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
thumbnail image: Folding-and-Assembly Strategy

Concerted folding and assembly processes are essential for protein self-assembly but have rarely been used in synthetic chemistry. Researchers have been aiming to develop an artificial folding-and-assembly strategy easily construct well-defined peptide pores from a short peptide fragment and a metal ion.


Makoto Fujita, University of Tokyo, Japna, and colleagues have synthesized porous peptide complexes by complexation of AgNTf2 and tripeptide ligands with a Gly-Pro-Pro sequence. The network of the polyproline II helices, found in collagen, gave 1.5-nm-sized pores, which could be modified by introduction of a proline analogue or functional groups.


High-resolution crystal structures revealed that the polyproline II helix conformation has a fine balance of structural fidelity and flexibility upon pore modifications. The resulting peptide-based pores could be used for molecular recognition or reactions.


 

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