Nawaz Afreen, Rai Gyan Prakash, Singh Kuljit, Shanker Asheesh, Ali Vahab
Laboratory of Molecular Biochemistry and Cell Biology, Department of Biochemistry, ICMR - Rajendra Memorial Research Institute of Medical Sciences (RMRIMS), Patna, Bihar, India.
Department of Bioinformatics, Central University of South Bihar, Gaya, Bihar, 824236, India.
Comput Biol Med. 2025 Apr;188:109753. doi: 10.1016/j.compbiomed.2025.109753. Epub 2025 Feb 12.
Visceral leishmaniasis poses a significant health challenge due to limited treatment options, drug resistance, and lack of vaccine. Targeting essential proteins of Leishmania parasites, either absent or distinct from human, is imperative for developing new chemotherapeutic strategies. The cysteine synthase (CS) and serine O-acetyltransferase (SAT) involved in the de novo cysteine biosynthetic pathway of L. donovani may represent an attractive drug target. This pathway is absent in humans and controls the trypanothione-based redox metabolism; crucial for parasite survival and drug resistance. The C-terminal SAT-peptides strongly bind to CS creating a regulatory CS-SAT complex, leading to partial or complete inhibition of CS activity. In this study, CS in complex with SAT was utilized as a framework to screen inhibitors against LdCS. Structure-based virtual screening and molecular docking against LdCS protein with varying precisions (SP and XP modes) were performed to identify potential novel inhibitors. We have identified 17 top-ranked hits exhibiting inhibitory activity based on docking score against LdCS. Four of these compounds were further evaluated through molecular dynamics simulations and biological assays. Compounds (ASN05106249) and (ASN03069898) showed significant inhibitory effect on CS enzymatic activity and growth of parasite that highlight the potential of LdCS to develop new therapies against Leishmaniasis.
由于治疗选择有限、耐药性以及缺乏疫苗,内脏利什曼病对健康构成了重大挑战。针对利什曼原虫中与人类不同或不存在的必需蛋白质,对于开发新的化疗策略至关重要。参与杜氏利什曼原虫从头合成半胱氨酸生物合成途径的半胱氨酸合酶(CS)和丝氨酸O-乙酰转移酶(SAT)可能是一个有吸引力的药物靶点。该途径在人类中不存在,并控制基于锥虫硫醇的氧化还原代谢;这对寄生虫的存活和耐药性至关重要。SAT的C末端肽与CS强烈结合,形成一个调节性的CS-SAT复合物,导致CS活性部分或完全受到抑制。在本研究中,与SAT复合的CS被用作筛选针对LdCS抑制剂的框架。针对LdCS蛋白进行了基于结构的虚拟筛选和不同精度(SP和XP模式)的分子对接,以鉴定潜在的新型抑制剂。我们已经根据对LdCS的对接分数鉴定出17个具有抑制活性的顶级命中物。其中四种化合物通过分子动力学模拟和生物学测定进行了进一步评估。化合物(ASN05106249)和(ASN03069898)对CS酶活性和寄生虫生长显示出显著的抑制作用,这突出了LdCS在开发抗利什曼病新疗法方面的潜力。