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 1 
Expression and Purification of Novel Peptide-Based Recombinant Proteins Targeting Breast Cancer Stem Cells Agusta, Istiqomah; Triwidyaningtyas, Silvia; Bela, Budiman; Mardiana, Mardiana; Wanandi, Septelia Inawati
Proceedings Book of International Conference and Exhibition on The Indonesian Medical Education Research Institute Vol. 9 No. - (2025): Proceedings Book of International Conference and Exhibition on The Indonesian M
Publisher : Writing Center IMERI FMUI

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.69951/proceedingsbookoficeonimeri.v9i-.327

Abstract

Introduction: Peptides with specific affinity toward breast cancer stem cells (BCSCs), including GYSASRSTIPGK and GAIRIRLSEPLS, have gained interest in targeted cancer diagnostics; however, the low abundance of BCSCs often results in limited detection sensitivity. This study addresses this limitation by conjugating BCSC-specific peptides to self-assembling Human Papillomavirus (HPV16) L1 protein, resulting in virus-like particles composed of 72 pentamers that provide substantial signal amplification. In addition, the SpyTag–SpyCatcher system derived from the Streptococcus pyogenes CnaB2 domain provides a robust strategy to enhance peptide–protein stability. Objectives: This study aimed to express and purify three recombinant proteins as key components for assembling a BCSC-specific diagnostic construct: HPV16 L1–SpyTag, SpyCatcher–GYSASRSTIPGK, and SpyCatcher–GAIRIRLSEPLS. Methods: Recombinant genes encoding the target proteins were expressed in Escherichia coli (E. coli) BL21(DE3) following IPTG induction for 1–4 hours. Bacterial cells were harvested and lysed under native or denaturing conditions, and recombinant proteins were purified using Ni-NTA affinity chromatography. Results: SDS–PAGE analysis showed clear bands at the expected molecular weights for HPV16 L1–SpyTag (58.5 kDa), SpyCatcher–GYSASRSTIPGK, and SpyCatcher–GAIRIRLSEPLS (~15 kDa), with induction-dependent increases in band intensity. The SpyCatcher–peptide fusions were predominantly soluble and purified under native conditions, whereas HPV16 L1–SpyTag was largely insoluble and required denaturing purification. Conclusion: HPV16 L1–SpyTag and SpyCatcher–peptide fusions were successfully expressed and purified in E. coli, establishing a versatile platform with potential to enhance BCSC-targeted detection and treatment strategies in breast cancer. 
Co-Authors Ade P.R. Simaremare Agusta, Istiqomah Andi Yasmon Andrijono Andrijono Anggraini Alam Anis Anis Ardiana Kusumaningrum Armi Susandi Aroem Naroeni Aroem Naroeni Ascobat, Purwantyastuti ASRI SULFIANTI Beti Ernawati Dewi Cahyani, Hesti Pramesti Christina, Diana Cintera Rahmagiarti Diah Iskandriati Dian Amirulloh Dimas Seto Prasetyo Dondin Sajuthi Elisna Syahruddin Evy Yunihastuti FERA IBIRAHIM Fera Ibrahim Firdaus Sirait Ganjar Noviar Gede Eko Darmono Geraldine, Vanessa Hanifi, Muhammad Hartiyowidi Yuliawuri Hartono, Soni Herna Herna Herna, Herna Hertanto, Robby Ibnu Agus Ariyanto Iin Maemunah Ingrid S. Surono Irawan, Priscilla Felicia Apriliani Jeanne Adiwinata Pawitan Jeanne Elvia Christian Kamila, Etri Dian Ketut Tuti Parwati Lili Indrawati Mardiana Mardiana Maria Lina R. Maria Lina Rosilawati Melinda Remelia Muhayya, Syarifah Raisha Murdani Abdullah Mursinah Mursinah Mursinah Mursinah Ni Ken Ritchie Ni Nengah Dwi Fatmawati Nia Kurniati Nuzli Fahdia Mazfufah Pamungkas, Joko Pauline Phoebe Halim Pramita Gayatri Pratiwi, Ekawati Betty Radiana Dhewayani Antarianto SAHLAN, MUHAMAD Sari, Siska Yuliana Satyapertiwi, Dwiantari SEPTELIA INAWATI WANANDI Silvia Tri Widyaningtyas Silvia Tri Widyaningtyas Silvia Tri Widyaningtyas Silvia Tri Widyaningtyas Silvia Tri Widyaningtyas Silvia Triwidyaningtyas Sofy Meilany Subangkit Subangkit Subiantistha, Tanaya Sugiarta, Gede Yuda SUWIJIYO PRAMONO Triwidyaningtyas, Silvia Utami, Mardhah Sastri VIVI SETIAWATY Widianingtyas, Silvia Widyaningtyas, Silvia Tri Wiseso, Anggoro Yohda, Masafumi YULIANTY MUHAYAR Yuliar Budi Hartanto Yusmaniar Yusmaniar Yuyun SM Soedarmono Yuyun Soedarmono Zakiudin Munasir