Biotinylated Peptides
Biotinylated Peptides - Related Videos
06:15
Biotinylated Cell-Penetrating Peptide Probe to Detect Protein-Protein Interactions
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2025
This video demonstrates a technique that uses biotinylated cell-penetrating peptides to detect intracellular protein-protein interactions. The cell-penetrating peptides facilitate the conjugated peptide to enter a cell and specifically bind to its interacting proteins. The biotin, after binding to avidin, allows purification of the interacting proteins’ complex from a cell lysate.
10:43
Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes
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2019
Here we present a method to select for novel variants of the E. coli biotin-protein ligase BirA that biotinylates a specific target peptide. The protocol describes the construction of a plasmid for the bacterial display of the target peptide, generation of a BirA library, selection and characterization of BirA variants.
09:13
Cell-surface Biotinylation Assay
0 Views •
2023
A cell can regulate the amount of particular proteins on its cell membrane through endocytosis, following which cell surface proteins are effectively sequestered in the cytoplasm. Once within a cell, these surface proteins can be either destroyed or “recycled” back to the membrane. The cell surface biotinylation assay provides researchers with a way to study these phenomena. The technique makes use of a derivative of the small molecule biotin, which can label surface proteins and then be...
10:26
Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
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Cited by 3 •
2017
This is a protocol to study intracellular protein-protein interactions based on the biotin-avidin pull-down system with the novelty of combining cell-penetrating sequences. The main advantage is that the target sequence is incubated with living cells instead of cell lysates and therefore the interactions will occur within the cellular context.
04:54
Evaluation of Controlled T Cell Activation with a Photoactivatable Peptide MHC
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2025
This video demonstrates a method of decaging a photoactivatable peptide-major histocompatibility complex using UV irradiation. The decaging process exposes the native peptide sequence, enabling precise T cell activation.
FAQs
Biotin provides a stable recognition site for avidin or streptavidin, which can be attached to a surface or linked to an enzyme, fluorophore, or nanoparticle. When a biotinylated peptide encounters these binding proteins, the interaction either immobilizes the peptide or produces a detectable signal. This dual use supports both enrichment-based assays and direct visualization.
Covalent attachment keeps biotin associated with the peptide during handling and assay steps, while the peptide’s defined amino acid sequence preserves its intended molecular features. Together, these properties help separate peptide-specific behavior from labeling variability. Researchers can therefore compare binding, signaling, or localization results across experiments using more reproducible molecular reagents.
Avidin or streptavidin can be used in two complementary formats. When presented on a coated surface, the binding proteins capture the peptide for interaction or purification studies. When conjugated to an enzyme, fluorophore, or nanoparticle, they reveal where the peptide is or whether binding occurred. The selected format determines whether the main outcome is capture, enrichment, or detection.
Their value comes from linking a defined peptide sequence to a controllable detection or capture step. This arrangement allows investigators to examine protein interactions, receptor binding, antigen recognition, and cell signaling while tracking the associated peptide. In this way, the reagent connects molecular binding behavior with broader cellular processes rather than serving only as a visual tag.
A biotinylated peptide can first be captured through its biotin by avidin or streptavidin associated with a coated surface or assay format. Material that interacts with the peptide can then be examined as part of an affinity purification or pull-down experiment. The resulting enrichment helps investigators investigate peptide-associated protein interactions using the sequence as the molecular probe.
They are useful when researchers need to determine where a peptide is associated within a biological system. A fluorophore- or nanoparticle-conjugated avidin or streptavidin reagent can bind the peptide’s biotin and provide a detectable label. This approach supports localization studies while retaining the peptide sequence needed to investigate receptor binding, antigen recognition, or signaling-related behavior.