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Rational Design of Peptide Binders Targeting Prominin‑1 and Sortilin for Molecular Sensing Applications
Samavath Mallawarachchi1, Nirmitee Mulgaonkar1, Samuel Mabbott2
1Department of Biological and Agricultural Engineering, Texas A&M University, College Station, Texas 77843, United States.
ACS Omega
|July 28, 2026
Summary
Researchers developed novel peptides targeting cancer biomarkers Prominin-1 (CD133) and sortilin. This peptide design approach offers a promising alternative to antibodies for cancer detection and treatment.
Area of Science:
- Biochemistry
- Molecular Biology
- Cancer Research
Background:
- Prominin-1 (CD133) and sortilin are key cancer biomarkers.
- Current antibody-based detection methods have limitations like glycosylation sensitivity and poor tumor penetration.
Purpose of the Study:
- To rationally design peptide-based targeting molecules for Prominin-1 and sortilin.
- To overcome limitations associated with antibody-based detection strategies.
Main Methods:
- Utilized a residue-level binding approach for peptide design.
- Employed molecular docking and molecular dynamics simulations for screening and stability verification.
- Validated peptide binding affinities using biolayer interferometry.
Main Results:
- Identified and designed peptides with predicted high binding affinities.
- Confirmed peptide binding to Prominin-1 and sortilin at micromolar levels.
- Observed consistent, albeit heterogeneous, binding for sortilin-targeting peptides.
Conclusions:
- The residue-level binding approach is effective for designing peptide binders against critical biomarkers.
- Developed peptides show potential as alternatives to antibodies for cancer biomarker targeting.
- This strategy offers a promising avenue for cancer diagnostics and therapeutics.
