In this section
@article{Saunders:2020:10.1021/acschembio.0c00328,
author = {Saunders, CN and Cota, E and Baum, J and Tate, EW},
doi = {10.1021/acschembio.0c00328},
journal = {ACS Chemical Biology},
pages = {1313--1320},
title = {Peptide probes for Plasmodium falciparum MyoA tail interacting protein (MTIP): exploring the druggability of the malaria parasite motor complex},
url = {http://dx.doi.org/10.1021/acschembio.0c00328},
volume = {15},
year = {2020}
}
TY - JOUR
AB - Malaria remains an endemic tropical disease, and the emergence of Plasmodium falciparum parasites resistant to current front-line medicines means that new therapeutic targets are required. The Plasmodium glideosome is a multiprotein complex thought to be essential for efficient host red blood cell invasion. At its core is a myosin motor, Myosin A (MyoA), which provides most of the force required for parasite invasion. Here, we report the design and development of improved peptide-based probes for the anchor point of MyoA, the P. falciparum MyoA tail interacting protein (PfMTIP). These probes combine low nanomolar binding affinity with significantly enhanced cell penetration and demonstrable competitive target engagement with native PfMTIP through a combination of Western blot and chemical proteomics. These results provide new insights into the potential druggability of the MTIP/MyoA interaction and a basis for the future design of inhibitors.
AU - Saunders,CN
AU - Cota,E
AU - Baum,J
AU - Tate,EW
DO - 10.1021/acschembio.0c00328
EP - 1320
PY - 2020///
SN - 1554-8929
SP - 1313
TI - Peptide probes for Plasmodium falciparum MyoA tail interacting protein (MTIP): exploring the druggability of the malaria parasite motor complex
T2 - ACS Chemical Biology
UR - http://dx.doi.org/10.1021/acschembio.0c00328
UR - https://pubs.acs.org/doi/10.1021/acschembio.0c00328
UR - http://hdl.handle.net/10044/1/79175
VL - 15
ER -
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