Peptide Science · 2020 · 15 citations · 24 references
PharmacyBiochemistryMedicinal ChemistryDrug DesignDrug DiscoveryStructural BiologyCombinatorial Peptide SynthesisPeptide ChemistryPeptide Drug DiscoveryPeptidomimetic DesignBioactive Peptide MimicsMedicinal Chemistry ApplicationsMicrowave-assisted Peptide SynthesisPeptide Coupling ReagentsPeptide Medicinal ChemistryPeptide StabilizationProtein Binding MotifSolid-phase Peptide Synthesis
Abstract The development of conformationally constrained analogues of bioactive peptides is a relevant goal in peptide medicinal chemistry. Among the several classes of conformationally constrained peptides, the so‐called stapled peptides, which bear a side‐chain‐to‐side‐chain bridge, are particularly interesting since they offer the possibility to stabilize specific conformational elements, such as α‐helices or β‐turns. We describe an efficient and reproducible microwave‐assisted strategy to prepare side‐chain‐to‐side‐chain clicked peptides, performing the copper‐catalyzed azide‐alkyne cycloaddition on solid phase, using as a model peptide a portion of the H1‐relaxin B chain, which contains the binding cassette motif of this important bioactive peptide. All the relevant parameters, that is, resin, solvent, catalytic system, microwave energy and reaction time were optimized using a systematic one‐factor‐at‐a‐time (OFAT) approach. This method will be useful for the preparation of libraries of conformationally constrained relaxin analogues.
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Steven A. Kawamoto, Adriana Coleska, Ran Xu et al. · Journal of Medicinal Chemistry · 2011 · 245 citations · Full text
Evolution of the relaxin-like peptide family
Tracey Wilkinson, Terence P. Speed, Geoffrey W. Tregear et al. · BMC Evolutionary Biology · 2005 · 199 citations · Full text