Biophysical Analysis of P. falciparum Heat Shock Protein 70-1 reveal features that make it amenable for drug design : Structural Dynamics of PfHsp70-1 for Targeted Antimalarial Drug Development

Malaria remains a global health challenge, with Plasmodium falciparum resistance to existing antimalarials increasing. The parasite's Heat Shock Protein 70 (PfHsp70-1) plays a critical role in protein folding and cytoprotection, making it a promising target for novel therapies. This study focuses on the structural and biophysical analysis of PfHsp70-1, particularly its nucleotide-binding domain (NBD), to evaluate its druggability. Using recombinant protein expression and purification, we characterized the NBD via circular dichroism (CD) spectroscopy, which confirmed its predominantly alpha-helical structure. Thermal stability assays indicated that the NBD remains structurally stable at elevated temperatures, with ATP presence marginally enhancing its stability. The results support the feasibility of developing ATP-mimetic inhibitors targeting PfHsp70-1, contributing to the next generation of antimalarial therapies.