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Pretargeted Radioimmunotherapy Based on the Inverse Electron Demand Diels-Alder Reaction

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Targeting Breast Cancer Using 177 Lu-Labeled Trastuzumab and Trastuzumab Fragment : First-in-Human Clinical

Yogesh Rathore¹, Tamanna Lakhanpal¹, Sudipta Chakraborty

¹From the Department of Nuclear Medicine, Post Graduate Institute of Medical Education and Research, Chandigarh.

Clinical Nuclear Medicine

|April 5, 2024

Summary

A new trastuzumab fragment (Fab) labeled with 177-Lutetium (Lu) shows promise for HER2-positive breast cancer theranostics. This fragment, 177Lu-DOTAGA-Fab, offers improved targeting and lower liver retention compared to the full antibody.

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Determining Binding Affinity KD of Radiolabeled Antibodies to Immobilized Antigens

Determining Binding Affinity KD of Radiolabeled Antibodies to Immobilized Antigens

Published on: June 23, 2022

Area of Science:

Nuclear medicine
Oncology
Immunotherapy

Background:

Trastuzumab is an antibody for HER2-positive breast cancer.
Large antibodies have slow pharmacokinetics and hepatobiliary clearance.
A smaller trastuzumab fragment (Fab) was developed for theranostics.

Purpose of the Study:

To evaluate the radiolabeling and targeting capabilities of a trastuzumab fragment (Fab) for HER2-positive breast cancer theranostics.
To compare the properties of 177Lu-DOTAGA-Fab with 177Lu-DOTAGA-trastuzumab.

Main Methods:

Fab was generated from trastuzumab via papain digestion.
Trastuzumab and Fab were conjugated with a bifunctional chelating agent (DOTA or DOTAGA).
Radiolabeling with 177Lu was performed, and affinity/specificity were assessed in vitro and in a first-in-human study.

Main Results:

DOTAGA conjugation yielded higher radiolabeling efficiency (83%) for Fab compared to trastuzumab (80.83%) under mild conditions.
177Lu-DOTAGA-Fab showed higher lesion uptake and lower liver retention than 177Lu-DOTAGA-trastuzumab.
177Lu-DOTAGA-Fab exhibited a faster washout from lesions (5 days) compared to the full antibody.

Conclusions:

177Lu-DOTAGA-Fab and 177Lu-DOTAGA-trastuzumab are suitable for targeting HER2 receptors.
The Fab fragment demonstrates favorable characteristics for theranostic applications in HER2-positive cancers.