Hsp40 Co-chaperones as Drug Targets: Towards the Development of Specific Inhibitors

Part of the Topics in Medicinal Chemistry book series (TMC, volume 19)


The heat shock protein 40 (Hsp40/DNAJ) family of co-chaperones modulates the activity of the major molecular chaperone heat shock protein 70 (Hsp70) protein group. Hsp40 stimulates the basal ATPase activity of Hsp70 and hence regulates the affinity of Hsp70 for substrate proteins. The number of Hsp40 genes in most organisms is substantially greater than the number of Hsp70 genes. Therefore, different Hsp40 family members may regulate different activities of the same Hsp70. This fact, along with increasing knowledge of the function of Hsp40 in diseases, has led to certain Hsp40 isoforms being considered promising drug targets. Here we review the role of Hsp40 in human disease and recent developments towards the creation of Hsp40-specific inhibitors.


Cancer Co-chaperone DNAJ Hsp40 Hsp70 Malaria Neurodegeneration 



Research activities in the laboratory of ALE are funded by the Cancer Association of South Africa (CANSA), Medical Research Council South Africa (MRC-SA), National Research Foundation (NRF) and Rhodes University. The views expressed are those of the authors and should not be attributed to CANSA, MRC-SA, NRF or Rhodes University. We have attempted to review the literature thoroughly, and we apologise if we have inadvertently missed any important contributions to the field.


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Copyright information

© Springer International Publishing Switzerland 2015

Authors and Affiliations

  1. 1.College of Health and BiomedicineVictoria UniversityMelbourneAustralia
  2. 2.Biomedical Biotechnology Research Unit, Department of Biochemistry, Microbiology and BiotechnologyRhodes UniversityGrahamstownSouth Africa

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