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Immunoglobulin-like Cell Adhesion Molecules

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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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Covalent Binding of Antibodies to Cellulose Paper Discs and Their Applications in Naked-eye Colorimetric Immunoassays

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Published on: October 21, 2016

Bioactive cellulose nanofibrils for specific human IgG binding.

Yanxia Zhang¹, Ruben G Carbonell, Orlando J Rojas

¹Departments of †Forest Biomaterials and ‡Chemical and Biomolecular Engineering, North Carolina State University , Raleigh, North Carolina 27695, United States.

Biomacromolecules

|October 18, 2013

Summary

This summary is machine-generated.

Researchers developed bioactive films using modified cellulose nanofibrils (CNF) conjugated with a peptide. These films show specific binding to human immunoglobulin G (hIgG), offering potential for diagnostic applications.

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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Area of Science:

Biomaterials Science
Nanotechnology
Surface Chemistry

Background:

Cellulose nanofibrils (CNF) offer a versatile platform for developing advanced biomaterials.
Immobilizing specific binding agents onto nanocellulose can create novel biosensing surfaces.
Controlling the surface chemistry of nanocellulose is crucial for functionalizing its properties.

Purpose of the Study:

To create bioactive films by conjugating a peptide with affinity for human immunoglobulin G (hIgG) onto modified cellulose nanofibrils (CNF).
To investigate two distinct methods for peptide grafting onto CNF-based structures.
To evaluate the hIgG binding capability and protein resistance of the developed peptide-modified CNF films.

Main Methods:

Grafting of poly(2-aminoethyl methacrylate hydrochloride-co-2-hydroxyethylmethacrylate) (poly(AMA-co-HEMA)) onto CNF via surface-initiated polymerization.
Immobilization of acetylated-HWRGWVA peptide onto the poly(AMA-co-HEMA) layer on CNF.
Characterization using atomic force microscopy (AFM) and scanning low energy electron microscopy.
Evaluation of hIgG binding and protein resistance using quartz crystal microgravimetry (QCM).

Main Results:

Two methods of peptide grafting (in suspension vs. on preformed film) were compared, yielding functionalized CNF networks.
The peptide-modified CNF films demonstrated specific binding affinity for hIgG.
The systems exhibited high signal-to-noise ratios, with investigated parameters affecting hIgG adsorption.
Non-specific protein resistance was also evaluated.

Conclusions:

Bioactive films can be successfully fabricated by conjugating peptides onto CNF using a grafted copolymer spacer.
The developed peptide-modified CNF platforms show promise for selective hIgG detection.
The study provides insights into optimizing peptide immobilization for enhanced biosensing performance.