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Issue 9, 2013
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Functional, metal-based crosslinkers for α-helix induction in short peptides

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Abstract

Many proteinprotein interactions that play a central role in cellular processes involve α-helical domains. Consequently, there has been great interest in developing strategies for stabilizing short peptides in α-helical conformations toward the inhibition and interrogation of proteinprotein interactions. Here, we show that tridentate hybrid coordination motifs (HCMs), which consist of a natural (histidine, His) and an unnatural (8-hydroxyquinoline, Quin) metal binding functionality, can bind divalent metal ions with high affinity and thereby induce/stabilize an α-helical configuration in short peptide sequences. The Quin functionality is readily introduced onto peptide platforms both during or after solid-state peptide synthesis, demonstrating the preparative versatility of HCMs. A systematic study involving a series of HCM-bearing peptides has revealed the critical importance of the length of the linkage between the Quin moiety and the peptide backbone as well as the metal coordination geometry in determining the extent of α-helix induction. Through ZnII coordination or modification with ReI(Quin)(CO)3, the HCM-bearing peptides can be rendered luminescent in the visible region, thus showing that HCMs can be exploited to simultaneously introduce structure and functionality into short peptides.

Graphical abstract: Functional, metal-based crosslinkers for α-helix induction in short peptides

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Supplementary files

Article information


Submitted
29 Mar 2013
Accepted
15 Jul 2013
First published
16 Jul 2013

Chem. Sci., 2013,4, 3740-3747
Article type
Edge Article

Functional, metal-based crosslinkers for α-helix induction in short peptides

S. J. Smith, K. Du, R. J. Radford and F. A. Tezcan, Chem. Sci., 2013, 4, 3740 DOI: 10.1039/C3SC50858G

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