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Targeted Cancer Therapies

Targeted Cancer Therapies

The targeted cancer therapies, also known as “molecular targeted therapies,” take advantage of the molecular and genetic differences between the cancer cells and the normal cells. It needs a thorough understanding of the cancer cells to develop drugs that can target specific molecular aspects that drive the growth, progression, and spread of cancer cells without affecting the growth and survival of other normal cells in the body.
There are several types of targeted therapies against...

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Initial Evaluation of Antibody-conjugates Modified with Viral-derived Peptides for Increasing Cellular Accumulation and Improving Tumor Targeting

Initial Evaluation of Antibody-conjugates Modified with Viral-derived Peptides for Increasing Cellular Accumulation and Improving Tumor Targeting

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Influence of Peptide-Based Chelator Sequences on HER2-Targeting Radiopeptide.

Sonal Gupta^1,2, Manoj Kumar¹, Krishna Mohan Repaka³

¹Radiopharmaceuticals Division, Bhabha Atomic Research Centre, Mumbai, India.

Journal of Peptide Science : an Official Publication of the European Peptide Society

|March 19, 2026

Summary

This summary is machine-generated.

Researchers developed a new technetium-99m (99mTc)-labeled peptide, [99mTc]Tc-CGGG-rL-A9, for targeting HER2-positive breast cancer. This radiolabeled peptide demonstrated high binding affinity and specificity in vitro and in vivo, showing potential for cancer detection and therapy.

Keywords:

HER2 receptors peptide‐based chelators rL‐A9 technetium‐99 m

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Area of Science:

Nuclear medicine
Radiopharmaceutical chemistry
Oncology

Background:

Human Epidermal growth factor Receptor 2 (HER2) is a key target in breast cancer therapy.
Radiolabeled peptides offer targeted delivery for imaging and treatment.
Previous rL-A9 peptide showed promise, necessitating further development.

Purpose of the Study:

To design and evaluate a novel HER2-targeting radiolabeled peptide for 99mTc-labeling.
To assess the in vitro and in vivo performance of the developed radiopeptide.

Main Methods:

Conjugation of cysteine-based chelators (CGGG, CSSG, CEEG) to the rL-A9 peptide.
Radiolabeling with 99mTc and stability assessment.
In vitro cell binding assays using SKBR3 cells.
In vivo studies in tumor xenografted mice for biodistribution and tumor uptake.

Main Results:

[99mTc]Tc-CGGG-rL-A9 showed high stability, unlike other variants.
Demonstrated high binding affinity (Kd: 5.82 ± 0.92 nM) and specificity (63% blocking) for HER2-expressing cells.
Moderate tumor uptake (3.56 ± 0.81% ID/g at 1h) and high retention (82.8% at 3h) observed in vivo.
Good tumor-to-background ratios and specific tumor inhibition (52.6%) confirmed HER2 targeting.

Conclusions:

The 99mTc-labeled peptide [99mTc]Tc-CGGG-rL-A9 is a stable and specific HER2-targeting agent.
It shows significant potential for diagnostic imaging and therapeutic applications in HER2-positive breast cancer.
Further studies are warranted to explore its full clinical utility.