## 1 Introduction  
One of the key challenges facing world health today is cancer. An estimated 20 million new instances of cancer were detected globally in 2022, resulting in about 9.7 million deaths. In spite of advances in medical research and treatment, the number of people affected by cancer is still rising. One in five people will have cancer at some point in their lives, and one in nine men and one in twelve women will die from the disease. These alarming figures demonstrate the urgent need for more research and the development of effective medications to treat this pervasive condition [1]. Faced with the alarming increase in cancer cases worldwide, the search for new therapeutic targets, such as HSP90, is becoming crucial to develop more effective treatments. HSP90 (Heat Shock Protein 90) is a chaperone protein essential for the survival of cancer cells, as it stabilizes key proteins involved in tumor growth [2]. Targeting HSP90 with inhibitors disrupts these mechanisms, leading to the degradation of oncoproteins and the death of cancer cells. This therapeutic approach shows promising potential, particularly for cancers resistant to conventional treatments [3]. Recent discoveries regarding HSP90, particularly its isoforms HSP90\(\alpha\) and HSP90B1, have significant implications for cancer treatment, strengthening therapeutic strategies and potentially improving patient outcomes. These findings highlight the crucial role of HSP90 as a key regulator of cancer cell survival and proliferation. HSP90\(\alpha\), often overexpressed in various cancers, promotes cell growth and resistance to therapies by regulating cell death pathways [4]. Furthermore, HSP90B1 has been identified as a novel biomarker associated with poor prognosis in several cancer types, making it a potential therapeutic target [5]. HSP90 inhibitors, including dual-targeted ones, have shown promising results in preclinical studies, enhancing antitumor effects when combined with other treatments [6]. These inhibitors disrupt oncogenic pathways, leading to the degradation of proteins essential for tumor survival. However, despite this potential, challenges such as drug resistance and toxicity remain major obstacles to their clinical application. Thus, further research is essential to optimize these therapies and improve patient outcomes [4]. The benzimidazole scaffold, a versatile heterocyclic structure, plays a vital role in developing compounds with significant biological and pharmacological properties. First synthesized by [PERSON] in 1872 as 2,5- and 2,6-dimethylbenzimidazole [7], this structure gained prominence after the discovery of N-ribosyl-dimethylbenzimidazole, which acts as cobalt's axial ligand in vitamin B12 [8]. Over time, benzimidazole derivatives have shown immense value in medicinal chemistry, exhibiting a wide range of activities, including antiparasitic (e.g., _albedazole_), antiulcer (e.g., _omeprazole_), antihypertensive (e.g., _candesartan_), antihistamine (e.g., _bilastine_), anticancer (e.g., _bendamustine_), and antipsychotic effects [9; 10]. Chemically, _N-aryl-benzimidazole_ are classified as benzimidazole derivatives with an aryl group attached to the nitrogen atom in the imidazole ring. This structural modification distinguishes these compounds within the broader benzimidazole family, imparting specific physical and chemical properties that enhance biological interactions, particularly for HSP90 inhibition. The _N-aryl-benzimidazole_ class includes compounds known for their ability to inhibit the HSP90 protein [11; 12] However, despite their promising efficacy, some compounds in this family face challenges in terms of metabolic stability, selectivity, and potential toxicity [5; 13]. To address these issues, our study employs computational approaches to identify structural analogs that are predicted to retain the inhibitory potential of _N-aryl-benzimidazole_ compounds, with improved pharmacokinetic and safety profiles.