Abstract
G-quadruplexes (G4) are non-canonical nucleic acid structures with important implications in biology. Based on an α-helical fragment of the RHAU helicase that displays high specificity for parallel-stranded G-quadrplexes, herein we demonstrate its head-to-tail cyclization by a high-efficiency ligase. The cyclic peptide exhibits superior stability and binding affinity to a G-quadruplex, and can serve as an excellent investigational tool for chemical biology applications.
MeSH terms
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A549 Cells
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Cyclization
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DEAD-box RNA Helicases / chemistry
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DEAD-box RNA Helicases / metabolism*
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DNA / genetics
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DNA / metabolism*
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G-Quadruplexes*
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Humans
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Oldenlandia / enzymology
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism*
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Peptide Synthases / chemistry
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Peptides, Cyclic / chemical synthesis
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Peptides, Cyclic / metabolism*
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Protein Binding
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Protein Stability
Substances
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Peptide Fragments
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Peptides, Cyclic
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DNA
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DEAD-box RNA Helicases
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Peptide Synthases