The significance of resorcinol/resorcylate in the structure of anti-cancer therapeutics targeting Hsp90: Synthesis and structure-activity relationship (SAR) studies.
- July 5, 2021
- Posted by: rsispostadmin
- Categories: Biochemistry, IJRSI
International Journal of Research and Scientific Innovation (IJRSI) | Volume VIII, Issue V, May 2021 | ISSN 2321–2705
Garba Suleiman1 *, Muktari Isa Shago2, Abba Mohammed2, Mohammed Nuhu Alamai3
1Department of Chemistry, Faculty of Science, Yobe State University, Damaturu, Nigeria.
2Department of Biochemistry, Faculty of Science, Yobe State University, Damaturu, Nigeria.
3College of Health Science & Technology, Nguru, Yobe State, Nigeria.
Abstract
The number of people suffering from cancer has been increasing rapidly over the years, placing a huge burden on our societies. The development of heat shock protein (hsp) inhibitors, especially Hsp90 signifies an alternative method for cancer therapy. Thanks to the plenty of similar overlapping regions that exist between cancer and Hsp90, proteins associated with cancer have been able to regulate the expression of Hsp90 via heat shock fator-1 (HSF-1). Because of the relationship between Hsp90 with Cancer, Alzheimer and Parkinson’s diseases we will put more emphasis on synthetic methodologies, structure–activity relationships and the significance of structures containing resorcinol moiety targeting those disorders.
Keywords: Cancer, Hsp90 inhibitors, resorcinol, resorcylate, molecular chaperone.
Introduction
The development of heat shock protein 90 (Hsp90) inhibitors as anti-cancer therapeutic agents is one of the major areas of concern in medicinal chemistry (1). Cancer, a disease caused as a result of uncontrollable cell division, is the second most notable cause of death around the globe, which has, over the years, become one of the critical challenges for humanity in almost every part of the world. According to a recent report, cancer averagely causes over 500,000 deaths every year, with an estimated peak of around 13 million to be reached by 2030. Thanks to the plenty of similar overlapping regions between cancer and Hsp90, proteins associated with cancer have been able to regulate the expression of Hsp90 via heat shock factor-1 (HSF-1).
Heat shock protein 90 is a highly conserved molecular chaperone abundant in the cytoplasm of normal eukaryotic cells used in maintaining protein homeostasis. It is an ATP dependent member of a multi-chaperone complex responsible for the conformational maturation, stabilization, folding, and activation of the client proteins directly related to cancer metastasis. Such client proteins are typically cancer-relevant targets like kinases,
