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Related Experiment Video

Updated: Jan 16, 2026

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells

Published on: October 27, 2020

Investigating SMR Peptide Interactions with Breast Cancer-Associated Proteins.

Ming-Bo Huang¹, Purushottam B Tiwari², Aykut Üren²

¹Department of Microbiology, Biochemistry, and Immunology, Morehouse School of Medicine, Atlanta, GA 30310, USA.

International Journal of Molecular Sciences

|September 27, 2025

Summary

HIV Nef protein's SMR peptide binds Mortalin and Vimentin, proteins involved in breast cancer (BC) progression. Specific Mortalin peptides block this interaction, offering potential BC therapeutics by disrupting tumor cell processes.

Keywords:

Mortalin SMR peptide Vimentin peptide–protein interaction surface plasmon resonance (SPR)

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Area of Science:

Molecular Biology
Oncology
Virology

Background:

Breast cancer (BC) remains a significant cause of cancer mortality.
Mortalin and Vimentin are proteins implicated in BC progression and metastasis.
The Secretion Modification Region (SMR) peptide of HIV Nef protein binds Mortalin and Vimentin, potentially disrupting exosome release and offering therapeutic targets.

Purpose of the Study:

To investigate the binding interactions between the SMR peptide, Mortalin, and Vimentin.
To map the SMR binding sites on Mortalin and identify similar sites on Vimentin.
To explore the therapeutic potential of blocking SMR-Mortalin/Vimentin interactions in breast cancer.

Main Methods:

Surface Plasmon Resonance (SPR) to quantify binding affinities.
Co-immunoprecipitation (Co-IP) to confirm interactions in BC cell lines.
Western blot assays and scanning peptide mapping to identify binding sites and functional inhibition.

Main Results:

The full Nef protein showed high affinity for Vimentin (KD = 0.75 ± 1.1 nM) and Mortalin (KD = 3.16 ± 0.03 nM).
The SMR peptide bound Mortalin and Vimentin with micromolar affinities (KD = 6.63–20.73 µM).
Specific Mortalin-derived peptides (#61 and #62) bound the SMR domain, inhibited Nef activity, and blocked SMRwt binding to Mortalin and Vimentin.

Conclusions:

The SMR peptide interacts with specific sites on Mortalin and Vimentin, potentially disrupting Epithelial-Mesenchymal Transition (EMT) and tumor progression.
Mortalin-derived peptides can effectively block SMR interactions with Mortalin and Vimentin.
These findings suggest a novel therapeutic strategy for breast cancer targeting the SMR peptide interactions.