Supporting data on characterisation of linker switch mutants of heat shock protein 110 and canonical Hsp70.

Here, we present data on characterisation of the linker of Hsp110 (PfHsp70-z) relative to the linker of canonical Hsp70s in support of a co-published article [1]. The linker of PfHsp70-z was switched with that of canonical Hsp70s, represented by PfHsp70-1 (cytosolic counterpart of PfHsp70-z) and Hsp70/DnaK. The datasets represent comparative analyses of PfHsp70-z, PfHsp70-1, and DnaK, relative to their linker switch mutants; PfHsp70-z, PfHsp70-1, DnaK, respectively.

Design and synthesis of quinoline-pyrimidine inspired hybrids as potential plasmodial inhibitors.

Presently, artemisinin-based combination therapy (ACT) is the first-line therapy of Plasmodium falciparum malaria. With the emergence of malaria parasites that are resistant to ACT, alternative antimalarial therapies are urgently needed. In line with this, we designed and synthesised a series of novel N-(7-chloroquinolin-4-yl)-N'-(4,6-diphenylpyrimidin-2-yl)alkanediamine hybrids (6a-7c) and evaluated their inhibitory activity against the NF54 chloroquine-susceptible strain as a promising class of antimalarial compounds.

Characterisation of a unique linker segment of the Plasmodium falciparum cytosol localised Hsp110 chaperone.

Plasmodium falciparum expresses two essential cytosol localised chaperones; PfHsp70-1 and PfHsp70-z. PfHsp70-z (Hsp110 homologue) is thought to facilitate nucleotide exchange function of PfHsp70-1. PfHsp70-1 is a refoldase, while PfHsp70-z is restricted to holdase chaperone function.