Ptm Inhibitory Peptide
Ptm Inhibitory Peptide - Related Videos
05:21
A Peptide Microarray Technology for Specificity Profiling of Antibodies
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2025
This video demonstrates a technique that applies peptide microarray technology to profile the specificity of antibodies recognizing post-translational modifications (PTMs) on histone peptides. A microarray slide containing immobilized fluorophore-conjugated histone peptides with known PTM combinations is treated with target PTM-specific antibodies. This process helps identify the antibody's specificity for the target and its potential cross-reactivity with non-target PTMs.
09:47
Analysis of Histone Antibody Specificity with Peptide Microarrays
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Cited by 22 •
2017
This manuscript describes methods for applying peptide microarray technology to specificity profiling of antibodies that recognize histones and their post-translational modifications.
10:35
Production and Testing of Antimicrobial Peptides and Their Mimics
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2026
This protocol describes a method for producing and evaluating the antimicrobial activity and cytotoxicity of the cationic peptide Mel4 and peptide mimic RK758. By integrating chemical synthesis, recombinant expression, and standardized functional assays, it provides a streamlined workflow for the production and testing of peptides and small-molecule mimics.
06:26
PTM Based Tumor Microenvironment Monitoring: A Method for Tracking Changes in ECM Rigidity Using Tumor Spheroids
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2023
This protocol describes a technique for monitoring extracellular matrix rigidity changes by using particle-tracking microrheology (PTM). This is done by culturing 3D pancreatic tumor spheroids into ECM with embedded fluorescent probes for video particle-tracking and analysis.
09:50
Mapping Inhibitory Neuronal Circuits by Laser Scanning Photostimulation
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Cited by 6 •
2011
This paper introduces an approach of combining laser scanning photostimulation with whole cell recordings in transgenic mice expressing GFP in limited inhibitory neuron populations. The technique allows for extensive mapping and quantitative analysis of local synaptic circuits of specific inhibitory cortical neurons.
FAQs
Different inhibitory designs interrupt PTM regulation at different molecular points. A peptide may mimic the sequence normally recognized as a substrate, occupy an enzyme’s binding site, or prevent a modifying enzyme from recognizing its target protein. These alternatives determine whether the experiment primarily reduces the modification or redirects how protein regulation proceeds.
Selectivity comes from designing the peptide around the relevant substrate sequence, enzyme binding site, or recognition event rather than treating all modification reactions as equivalent. This focused interference helps researchers attribute an observed cellular change to a particular PTM-controlled process, supporting clearer analysis of signaling pathways and protein regulation.
Blocking recognition can interrupt regulation even when the modifying enzyme remains present in the cell. By preventing the enzyme from engaging its target protein, the peptide helps separate the role of that interaction from the enzyme’s broader presence or activity. This is useful for examining how a specific PTM contributes to signaling or cellular behavior.
Researchers can examine the relevant modification after peptide-mediated interference and relate any accompanying change in cellular behavior to that altered regulation. The approach is most informative when the modification, its controlling interaction, and the resulting biological response are considered together, allowing a more focused assessment of the PTM’s functional contribution.
They can help clarify whether phosphorylation, acetylation, ubiquitination, or another PTM participates in a signaling pathway, rather than merely occurring alongside it. By selectively interfering with the controlling interaction, researchers can investigate links between protein modification and cellular behavior, providing biological context for how regulatory pathways influence cell function.
Their selectivity provides a way to probe protein-regulatory events associated with disease without treating every PTM as functionally identical. Findings can reveal whether a particular modification or recognition step influences cellular behavior, while also informing development of peptide-based tools for modulating protein function and investigating disease-related regulatory mechanisms.