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Updated: May 3, 2026
Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes
Published on: October 3, 2019
Serine and proline-rich ligands enriched via phage-display technology show preferential binding to BCR/ABL expressing
Karen Shires1, Iva Shankland2, Shaheen Mowla3
1National Health Laboratory Services (NHLS)/Groote Schuur Hospital, Haematology, Cape Town, South Africa; Division of Haematology, University of Cape Town, Cape Town, South Africa.
Background And Objectives:
Despite the use of targeted therapy, chronic myelogenous leukemia (CML) currently remains incurable with drug therapy, with patients requiring life-long treatment. Developing either a vaccine to prevent the disease or another novel drug to specifically target and eradicate the CML cell will require the identification of CML-associated cell-surface markers and molecules that can bind specifically to the cell surface. In an attempt to discover peptides that bind specifically to cells in the early chronic phase of the disease, we used phage-display technology to identify heptapeptides that bind specifically to the surface of BCR/ABL-expressing fibroblasts.
Methods:
An in vitro system using NIH3T3 stably transfected with pGD210 (BCR/ABL) was used as a model for the chronic phase of the disease. The cells were panned using a linear heptapeptide phage library (Ph.D 7.0) in a negative/positive panning strategy with NIH3T3 containing only the plasmid vector as the wild type control.
Results:
We identified four novel peptides that were enriched through this technique. These peptides contained either multiple proline residues or serine/threonine-proline pairs and showed a confirmed binding preference for BCR/ABL+ fibroblasts. The peptide Y-R-A-P-W-P-P also showed a binding affinity for granulocytes from untreated CML patients.
Conclusion:
We have identified several novel peptides that can be used in future studies to identify specific CML cell-surface antigens or provide a novel drug-delivery mechanism.
Insights
Researchers identified novel peptides that bind to chronic myelogenous leukemia (CML) cells. These peptides may aid in developing new CML therapies or diagnostic tools for the incurable blood cancer.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Chronic myelogenous leukemia (CML) remains incurable with current drug therapies, necessitating lifelong treatment.
- Developing novel treatments like vaccines or targeted drugs requires identifying CML-specific cell surface markers.
- Effective CML eradication strategies depend on molecules that bind specifically to CML cells.
Purpose of the Study:
- To discover novel heptapeptides that specifically bind to the surface of BCR/ABL-expressing fibroblasts, modeling early chronic phase CML.
- To identify potential therapeutic targets or drug delivery mechanisms for CML.
Main Methods:
- Utilized phage-display technology with a linear heptapeptide library (Ph.D 7.0).
- Employed a negative/positive panning strategy using BCR/ABL-transfected NIH3T3 cells and control cells.
- In vitro system modeled the chronic phase of CML.
Main Results:
- Identified four novel heptapeptides enriched through the panning process.
- These peptides feature proline-rich sequences or serine/threonine-proline pairs.
- One peptide, Y-R-A-P-W-P-P, demonstrated binding affinity for granulocytes from CML patients.
Conclusions:
- Several novel peptides with specific binding properties to CML-associated cells were discovered.
- These identified peptides represent potential candidates for future CML cell-surface antigen identification.
- The peptides may serve as a basis for novel drug-delivery systems in CML treatment.
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