Cd47 Peptide Immobilization
Cd47 Peptide Immobilization - Related Videos
08:13
Mitigation of Blood Borne Cell Attachment to Metal Implants through CD47-Derived Peptide Immobilization
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Cited by 2 •
2020
Presented here is a protocol for appending peptide CD47 (pepCD47) to metal stents using polybisphosphonate chemistry. Functionalization of metal stents using pepCD47 prevents the attachment and activation of inflammatory cells thus improving their biocompatibility.
06:15
Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion
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Cited by 9 •
2016
Cell-adhesiveness is key to many approaches in biomaterial research and tissue engineering. A step-by-step technique is presented using wet-chemistry for the surface modification of the important polymer PTFE with peptides.
03:21
Peptide Purification: An RP-HPLC-based Technique to Extract Peptides from Digested Protein Lysates
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2023
In this video, we demonstrate reversed-phase high-performance liquid chromatography to purify peptides from a digested protein lysate mixture. These purified peptides are then lyophilized and stored for downstream applications. Analysis of peptides can help understand the mechanics involved in cellular signaling and cancer.
02:12
Inducing Depression-like Behavior in a Mouse via Immobilization Stress
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2025
This video demonstrates the method of inducing chronic stress in a mouse through repeated immobilization, leading to corticosterone release and reduced glutamate receptor activity in neurons, which results in depression-like behavior.
04:00
Immunoaffinity Based Extraction of Ubiquitinylated Peptides: A Technique to Selectively Extract Ubiquitin Tagged Peptides from Purified Peptide Fractions
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2023
This video describes a method to extract and purify ubiquitinylated peptides containing remnant di-glycine peptides from a complex peptide mixture. The presented method may help in identifying original ubiquitination sites in the protein.
FAQs
The main parameters are peptide density, orientation, and accessibility at the engineered interface. Density determines how many ligands are presented, while orientation and accessibility influence whether SIRPα on immune cells can physically interact with them. Controlling these variables allows researchers to tune the strength and consistency of the cell-protective signal produced by the material.
When the immobilized peptide interacts with SIRPα on immune cells, it can reduce cellular recognition and phagocytic clearance. This matters because immune-cell behavior strongly influences how a material, nanoparticle, or cell-based construct persists in a biological setting. The interface therefore acts not only as a physical surface but also as a regulator of immune communication.
Covalent coupling anchors the peptide directly to the biomaterial or engineered interface, creating a defined presentation of the ligand rather than relying on an unstructured surface association. Because the attachment can be designed alongside density, orientation, and accessibility, the resulting system provides a tunable way to investigate how surface presentation affects cell-material interactions.
Design should account for the amount of peptide attached, how each peptide is oriented, and whether its SIRPα-interacting region remains accessible. These variables are interconnected: a surface may contain peptide but still provide limited signaling if the ligand is poorly presented. Systematic control helps distinguish effects caused by peptide presence from effects caused by its surface organization.
A general workflow begins by selecting the biomaterial or engineered interface, followed by covalent coupling of the CD47-derived peptide. Researchers then control or characterize peptide density, orientation, and accessibility because these features determine how the surface presents the ligand. The finished construct can be examined as a platform for studying cell-material interactions and immune-related behavior.
The strategy can be incorporated into biomaterials, nanoparticles, and cell-based constructs. In these settings, the intended outcome is improved biocompatibility and reduced immune recognition or phagocytic clearance, which may support greater construct persistence. It also offers a design route for immune-evasive therapeutic systems rather than treating immune interactions as an unavoidable property of the material.
Tuning the interface helps researchers examine how ligand density, orientation, and accessibility shape interactions between engineered materials and immune cells. These comparisons can connect surface design to reduced recognition, lower phagocytic clearance, biocompatibility, and persistence. The approach therefore serves both as a materials-engineering strategy and as an experimental platform for analyzing cell-material communication.