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Introduction <p>Latent membrane protein1 (LMP1) is a ligand-independent receptor overexpressed in EBV-associated malignancies. The Phage Display approach has been extensively employed to identify peptides targeting proteins or receptors involved in pathways dysregulated in cancer.</p> Material and Methods <p>We use HeLa cells, transfected with LMP1, as targets to screen for LMP1 specific peptides using a phage display library.</p> Results <p>After four rounds of biopanning, 11 peptides were selected based on their binding affinity to the extracellular region of LMP1. Among the selected peptides, two (PEP-7 and PEP-11) exhibited the highest interaction energy scores by Molecular docking with the LMP1 protein. Furthermore, based on NCBI protein database, PEP-7 and PEP-11 showed similarities with proteins (TNFR and SNW1) involved in the NFkB pathway in which LMP1 is strongly engaged.</p> Conclusion <p>We selected by Phage Display two LMP1-targeting peptides that proved interaction with their target by Molecular Docking. Further in vivo and in vitro investigations are needed to better elucidate the functions of these peptides and to validate their utility in EBV-associated malignancies’ diagnosis and therapy.</p>

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Selection of Peptides Targeting the LMP1 Oncoprotein Via Phage Display Differential Screening on Cancer Cells

  • 期刊论文

  • 发表日期：

    2025年2月17日

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  • Nihel Ammous-Boukhris,
  • Nedra Rached,
  • Amor Mosbah,
  • Wajdi Ayadi,
  • Ali Gargouri,
  • Raja Mokdad-Gargouri

摘要

Introduction

Latent membrane protein1 (LMP1) is a ligand-independent receptor overexpressed in EBV-associated malignancies. The Phage Display approach has been extensively employed to identify peptides targeting proteins or receptors involved in pathways dysregulated in cancer.

Material and Methods

We use HeLa cells, transfected with LMP1, as targets to screen for LMP1 specific peptides using a phage display library.

Results

After four rounds of biopanning, 11 peptides were selected based on their binding affinity to the extracellular region of LMP1. Among the selected peptides, two (PEP-7 and PEP-11) exhibited the highest interaction energy scores by Molecular docking with the LMP1 protein. Furthermore, based on NCBI protein database, PEP-7 and PEP-11 showed similarities with proteins (TNFR and SNW1) involved in the NFkB pathway in which LMP1 is strongly engaged.

Conclusion

We selected by Phage Display two LMP1-targeting peptides that proved interaction with their target by Molecular Docking. Further in vivo and in vitro investigations are needed to better elucidate the functions of these peptides and to validate their utility in EBV-associated malignancies’ diagnosis and therapy.