Eka Pratiwi, Eka Odja Anggraeni, Andi Besse Khaerunisa, Andi Muhammad Anshar, Bulkis Musa, Rizal Irfandi, Fredryk W Mandey, Erna Mayasari, Andi Adillah Nur Syafirah, Wildan Mubaraq, Indah Raya
Objective: Cisplatin-based chemotherapy remains a widely used treatment for breast cancer, whether administered orally or intravenously. However, its clinical effectiveness is limited by poor selectivity, severe side effects, systemic toxicity, and the emergence of drug resistance. To overcome these limitations, this study investigates a novel molecular complex-Zn(II)-Cysteine-Tyrosine dithiocarbamate as a potential alternative with improved safety and efficacy in breast cancer therapy. Methods: The complex was synthesized via a reaction involving zinc metal, cysteine, carbon disulfide (CS2), potassium hydroxide (KOH), and tyrosine. It underwent comprehensive physicochemical characterization using Fourier-transform infrared (FT-IR) spectroscopy, UV-Vis spectroscopy, scanning electron microscopy with energy-dispersive X-ray spectroscopy (SEM-EDS), X-ray diffraction (XRD), melting point analysis, and electrical conductivity measurements. The compound’s anticancer activity was evaluated in vitro against MCF-7 breast cancer cells. In addition, molecular docking was performed to assess binding interactions with Estrogen Receptor α. Results: The synthesis achieved an 88.1% yield, with a melting point of 202-204°C and a conductivity of 0.4 mS/cm. In vitro analysis revealed morphological changes consistent with apoptosis at concentrations ≥250 µg/mL, and the IC50 value was determined to be 511.40 µg/mL. Molecular docking indicated strong binding affinity between the complex and Estrogen α, with a binding energy of -75.41 kJ/mol. Key amino acid residues involved in the interaction included Lys449, Phe495, Ile389, Ile514, Met388, Glu385, Leu387, and Gly390. Both hydrophobic interactions and hydrogen bonding contributed to the complex’s structural stability. Conclusion: Although the Zn (II)-Cysteine-Tyrosine dithiocarbamate complex demonstrated limited cytotoxic activity, its strong binding interactions and molecular stability suggest potential for further structural optimization. These findings offer valuable insights into the relationship between molecular architecture and anticancer behavior, laying the groundwork for future therapeutic development. © 2025 Asia Pacific Journal of Cancer Prevention. This work is licensed under a Creative Commons Attribution-Non Commercial 4.0 International License.
Department of Chemistry, Faculty of Mathematics and Natural Science, Hasanuddin University, Makassar, 90245, Indonesia; Department of Chemistry, Faculty of Mathematics and Natural Science, Universitas Negeri Makassar, Jalan Daeng Tata Raya Makassar, Makassar, 90244, Indonesia; Life Environment Conservation Science, Ehime University, Indonesia; Faculty of Medicine, Hasanuddin University, Makassar, 90245, Indonesia
Research at a Glance
Register to unlock
Topics & SDG Alignment
Register to unlock
Collaboration
Register to unlock
Author Profile (Selected)
Register to unlock
References Overview
Register to unlock
Journal & Source
Register to unlock
Metadata & Integrity
Register to unlock