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Immunogold Electron Microscopy

Immunogold Electron Microscopy

Immunoelectron microscopy utilizes immunogold labeling of endogenous proteins with specific antibodies to detect and localize these proteins in cells and tissues. The procedure provides insights into the distribution and quantification of protein under different stimulation conditions offering clues about their functions. Conjugating highly electron-dense gold particles with primary or secondary antibodies allow antigen detection on and within cells, with high resolution and specificity.

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Related Experiment Video

Updated: Jun 5, 2026

Murine Lymphocyte Labeling by 64Cu-Antibody Receptor Targeting for In Vivo Cell Trafficking by PET/CT

Murine Lymphocyte Labeling by ⁶⁴Cu-Antibody Receptor Targeting for In Vivo Cell Trafficking by PET/CT

Published on: April 29, 2017

Chelator-Free Radiometal Labeling Inside Engineered Affibodies.

Lani J Davies¹, Upamali Somathilake¹, Santhanalaxmi Kumaresan¹

¹Research School of Chemistry, Australian National University, Canberra, Australia.

Angewandte Chemie (International Ed. in English)

|June 4, 2026

Summary

This summary is machine-generated.

Researchers developed a novel method to directly incorporate metals into affibody proteins, eliminating the need for linkers. This innovation enables targeted cancer therapies and imaging using affibody-metal complexes.

Keywords:

affibody alpha particle bismuth helix bundle radiolabel

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Area of Science:

Biotechnology
Protein Engineering
Radiochemistry

Background:

Affibody proteins are stable three-helix bundles engineered for specific protein binding.
Current methods use bifunctional linkers to attach chelators for metal incorporation in affibodies.
Metal-affibody conjugates are used in cancer imaging and therapy.

Purpose of the Study:

To develop a linker-free method for metal incorporation into affibody proteins.
To create stable and functional affibody-metal complexes for biomedical applications.
To evaluate the potential of bismuth-loaded affibodies for HER2-targeted cancer therapy.

Main Methods:

Engineered a triple cysteine motif within the affibody core to bind metal ions.
Tested binding and stability of various metal-affibody complexes (Bi(III), Pb(II), In(III), Ga(III)).
Assessed complex integrity against glutathione and strong chelators.
Evaluated the binding affinity of a bismuth-loaded affibody to the HER2 receptor.
Demonstrated targeted delivery of bismuth-213 to HER2-overexpressing cancer cells.

Main Results:

A simple triple cysteine motif enabled direct and stable binding of Bi(III), Pb(II), In(III), and Ga(III).
Metal uptake was instantaneous at room temperature and physiological pH.
Affibody-metal complexes remained intact for one week at 4°C and resisted glutathione.
The bismuth-affibody complex showed high stability against strong chelators.
Bismuth-loaded affibody retained HER2 binding affinity and selectively delivered bismuth-213 to cancer cells.

Conclusions:

Engineered affibodies can directly bind and retain therapeutic or imaging metals without linkers.
This linker-free approach offers a stable and efficient platform for developing targeted radiopharmaceuticals.
Bismuth-loaded affibodies show promise for targeted alpha therapy of HER2-overexpressing cancers.