Search research articles

Search research articles

Related Experiment Videos

Solid phase assembly of defined protein conjugates.

John C Russell¹, Tracey L Colpitts, Shelley R Holets-McCormack

¹D09FQ, AP20, Abbott Laboratories, 100 Abbott Park Road, Abbott Park, Illinois 60064-6015, USA. john.c.russell@abbott.com

Bioconjugate Chemistry

|September 19, 2002

Summary

This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

AI-enhanced X-ray microscopy for non-destructive detection, quantification, and particle size analysis of crystalline miconazole in amorphous solid dispersions.

Journal of pharmaceutical sciences·2025

Same author

General Surgery Resident Participation in a Mandatory Wellness Program: Six Years Later.

The Journal of surgical research·2024

Same author

PAUSE: principled feature attribution for unsupervised gene expression analysis.

Genome biology·2023

Same author

Effect of a behavioral intervention on anxiety and perceived performance of non-technical skills during surgical simulations.

American journal of surgery·2021

Same author

Disparities of Single-Particle Growth Rates in Buried Versus Exposed Ritonavir Crystals within Amorphous Solid Dispersions.

Molecular pharmaceutics·2020

Same author

More Than Aligning Perception: Impact of an Educational Intervention on Medical Student Mistreatment Reporting.

Journal of the American College of Surgeons·2020

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

We developed a novel solid-phase method for protein-protein conjugation, enabling precise control over conjugate size and composition. This technique creates uniform, custom-sized protein complexes for various applications.

Area of Science:

Bioconjugation Chemistry
Protein Engineering
Materials Science

Background:

Traditional protein-protein conjugation methods often lack control over product size and homogeneity.
Developing methods for precisely assembling protein conjugates is crucial for applications in diagnostics and therapeutics.

Purpose of the Study:

To develop a solid-phase procedure for protein-protein conjugation offering enhanced control over product size and composition.
To demonstrate the versatility of the method by preparing conjugates with specific sizes and component arrangements.

Main Methods:

A stepwise solid-phase assembly approach was employed, sequentially adding activated proteins to a support.
The quantity of the first protein bound to the support determined the total number of conjugate units.

Related Experiment Videos

Conjugates were released from the support by cleaving a linker, and characterized using size-exclusion chromatography and atomic force microscopy.

Main Results:

The developed method yielded uniformly sized protein conjugates with controlled composition and component placement.
A series of conjugates were successfully prepared, featuring R-phycoerythrin as the central protein, with alkaline phosphatase and IgG, ranging from 1.6 to 11.5 MDa.
Size-exclusion chromatography and atomic force microscopy confirmed the homogeneity and controlled size of the prepared conjugates.

Conclusions:

The novel solid-phase conjugation procedure provides superior control over conjugate size, composition, and structure compared to existing methods.
The prepared protein conjugates demonstrated performance consistent with their defined compositions in an immunoassay for human thyroid stimulating hormone.
This technique offers a versatile platform for creating well-defined protein assemblies for advanced biotechnological applications.