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Biotechnology Information
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R&D Systems
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Abbott Laboratories
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Pfizer Inc
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Thermo Fisher
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Beyotime
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Journal: bioRxiv
Article Title: A Computational Workflow for Structure-Guided Design of Potent and Selective Kinase Peptide Substrates
doi: 10.1101/2025.07.04.663216
Figure Lengend Snippet: Experimental validation of designed peptides shows improved kinase activity. ( A ) ADP-Glo assay baseline measurements showing kinase activity with parental substrates and background controls for all five tested kinases. ( B–F ) Relative percentage change in kinase activity for designed peptides compared to parental substrates for ALK ( B ), MET ( C ), ROS1 ( D ), EGFR L858R ( E ), and SRC ( F ). Designed peptides are color-coded with sequence information provided. Phosphosite residues that were fixed during design are highlighted in green. Four out of five kinases showed substantial activity improvements with at least one designed peptide.
Article Snippet: The
Techniques: Biomarker Discovery, Activity Assay, Glo Assay, Sequencing, Phospho-proteomics
Journal: bioRxiv
Article Title: A Computational Workflow for Structure-Guided Design of Potent and Selective Kinase Peptide Substrates
doi: 10.1101/2025.07.04.663216
Figure Lengend Snippet: Kinetic characterization reveals improved binding affinity of designed peptides. ( A ) Schematic of kinase phosphorylation reaction monitored by the LIMS-kinase assay. ( B ) Multiple reaction monitoring (MRM) setup showing the mass spectrometry detection pathway for ADP quantification. ( C–E ) Michaelis-Menten kinetic analysis comparing parental and optimized peptides for ROS1 ( C ), MET ( D ), and ALK ( E ). Left panels show time-course data at varying substrate concentrations; right panels show saturation curves with fitted K m values and 95% confidence intervals. The designed peptides demonstrated lower K m values, indicating improved apparent binding affinity.
Article Snippet: The
Techniques: Binding Assay, Phospho-proteomics, Kinase Assay, Targeted Proteomics, Mass Spectrometry
Journal: bioRxiv
Article Title: A Computational Workflow for Structure-Guided Design of Potent and Selective Kinase Peptide Substrates
doi: 10.1101/2025.07.04.663216
Figure Lengend Snippet: Structural analysis reveals molecular basis for improved activity. ( A-D ) Comparison of AlphaFold-Multimer predicted structures and hydrogen bonding networks for parental (green) versus designed (yellow) peptides in complex with ALK ( A ), ROS1 ( B ), MET ( C ), and EGFR L858R ( D ). Kinase structures are shown in gray ribbon representation. Green boxes highlight hydrogen bond interactions formed by parental peptides; yellow boxes show interactions formed by designed peptides. Designed peptides generally form additional or optimized hydrogen bonds that correlate with improved experimental activity.
Article Snippet: The
Techniques: Activity Assay, Comparison