Year: 2026
Type: article
Abstract: Candida albicans is an opportunistic fungal pathogen that participates in the life-threatening bloodstream infections. Although the virulent nature of the fungus has been well studied, targeting its druggability for therapeutics still requires extensive research. The special structural morphogenesis known as the hyphae leads to pathogenic biofilm formation by the organism. Pkc1 is the kinase protein involved in hyphae formation. Pkc1 is a client kinase that binds to the co-chaperone Cdc37. This Cdc37-Pkc1 complex then associates with the Hsp90 chaperone machinery. Together, Hsp90 and Cdc37 stabilize and activate the Pkc1 protein for proper cell integrity signalling. When Hsp90 loses control over Pkc1, the client protein participates in hyphal development through the CWI pathway. The main focus is on the interaction of Cdc37 and Pkc1; the Pkc1 protein binds to the N-terminal domain of Cdc37. Molecular docking studies of the Cdc37 protein with FDA-approved ligands targeting its N-terminal domain may inhibit the formation of the Cdc37–Pkc1 complex. Among the approved drugs we found that Nilotinib shows the best binding affinity towards the domain-specific inhibition of Cdc37.
Institutions: JIS University, University of Kalyani
Language: English
Subfield: Drug Discovery
Domain: Life Sciences
Open Access status: bronze
Funder: University of Kalyani
OpenAlex ID: W7203744810