ArticleChemical science2013
Functional, metal-based crosslinkers for α-helix induction in short peptides.
Article in Chemical science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Peptide structure and silver ion affinity: influence on the formation of α-helices upon metal binding.Chemical communications (Cambridge, England) · 2026Article
- A glutamine-based single α-helix scaffold to target globular proteins.Nature communications · 2022Article
- Dual Control of Peptide Conformation with Light and Metal Coordination.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Folding of unstructured peptoids and formation of hetero-bimetallic peptoid complexes upon side-chain-to-metal coordination.Chemical science · 2019Article
- Tunable Helicity, Stability and DNA-Binding Properties of Short Peptides with Hybrid Metal Coordination Motifs.Chemical science · 2016Article
- Micelle-Triggered β-Hairpin to α-Helix Transition in a 14-Residue Peptide from a Choline-Binding Repeat of the Pneumococcal Autolysin LytA.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- Enzyme-catalyzed macrocyclization of long unprotected peptides.Organic letters · 2014Article
- Convergent diversity-oriented side-chain macrocyclization scan for unprotected polypeptides.Organic & biomolecular chemistry · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Many protein-protein 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 protein-protein 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 Zn
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.