Therapeutic Potential of Heat Shock Protein 90 Inhibitors, Geldanamycin, and Analog Compounds in Precision Cancer Therapy
Heat shock protein (HSP90) is a molecular chaperone involved in numerous physiological processes. The primary role of this is to assist in the process of protein folding and to restore misfolded proteins to their correct shape. Chaperones additionally inhibit protein breakdown and aggregation. HSP90...
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2023-12-01
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author | Atta Mohammed Alzebari Amjad Mahmood Qadir Mahmood Sherzad Rafaat Abbas Salihi |
author_facet | Atta Mohammed Alzebari Amjad Mahmood Qadir Mahmood Sherzad Rafaat Abbas Salihi |
author_sort | Atta Mohammed Alzebari |
collection | DOAJ |
description | Heat shock protein (HSP90) is a molecular chaperone involved in numerous physiological processes. The primary role of this is to assist in the process of protein folding and to restore misfolded proteins to their correct shape. Chaperones additionally inhibit protein breakdown and aggregation. HSP90 inhibitors possess a notable characteristic of obstructing many cancer-causing pathways by facilitating the breakdown of numerous oncogenic client proteins. Targeting HSP90 therapeutics has been recognized as a viable approach for treating cancer and inflammatory-associated disorders in clinical studies involving different forms of cancer. Inhibition of HSP90 using natural, synthetic, and semi-synthetic chemicals has shown encouraging outcomes. HSP90 inhibitors have been extracted from several fungi, bacteria, and plant species. These naturally occurring chemicals play a crucial function in regulating HSP90 activity and can be utilized to develop innovative semi-synthetic or synthetic inhibitors. Over 120 clinical trials have been carried out to evaluate the effectiveness of HSP90 inhibitors as a supplementary therapy for different types of tumor cells. Presently, ongoing research is being carried out to acquire an understanding of innovative and more efficacious methods for treating cancer. Continuing in this research approach, we aim to investigate the discovery, biosynthesis, mechanism of action, and biological features of geldanamycin and its analogs. |
format | Article |
id | doaj-art-ebfbfad8aade4160ba3bbf90643f9262 |
institution | Kabale University |
issn | 2960-1428 |
language | English |
publishDate | 2023-12-01 |
publisher | QAASPA Publisher |
record_format | Article |
series | BioMed Target Journal |
spelling | doaj-art-ebfbfad8aade4160ba3bbf90643f92622025-01-10T21:54:26ZengQAASPA PublisherBioMed Target Journal2960-14282023-12-011222110.59786/bmtj.12217Therapeutic Potential of Heat Shock Protein 90 Inhibitors, Geldanamycin, and Analog Compounds in Precision Cancer TherapyAtta Mohammed Alzebari0https://orcid.org/0009-0004-5668-5982Amjad Mahmood Qadir1https://orcid.org/0000-0002-4142-6118Mahmood Sherzad Rafaat2https://orcid.org/0000-0002-3439-6686Abbas Salihi3https://orcid.org/0000-0002-1342-2849Chemical Biology Group, Institute of Organic and Macro Molecular Chemistry, Friedrich Schiller University-Jena, 07737 Jena, GermanyDepartment of General Science, College of Basic Education, University of Halabja, 46018 Halabja, KRG, IraqPathological Analysis Department, Paytakht Technical Institute, Erbil, 44001, IraqDepartment of Biology, College of Science, Salahaddin University-Erbil, 44001, IraqHeat shock protein (HSP90) is a molecular chaperone involved in numerous physiological processes. The primary role of this is to assist in the process of protein folding and to restore misfolded proteins to their correct shape. Chaperones additionally inhibit protein breakdown and aggregation. HSP90 inhibitors possess a notable characteristic of obstructing many cancer-causing pathways by facilitating the breakdown of numerous oncogenic client proteins. Targeting HSP90 therapeutics has been recognized as a viable approach for treating cancer and inflammatory-associated disorders in clinical studies involving different forms of cancer. Inhibition of HSP90 using natural, synthetic, and semi-synthetic chemicals has shown encouraging outcomes. HSP90 inhibitors have been extracted from several fungi, bacteria, and plant species. These naturally occurring chemicals play a crucial function in regulating HSP90 activity and can be utilized to develop innovative semi-synthetic or synthetic inhibitors. Over 120 clinical trials have been carried out to evaluate the effectiveness of HSP90 inhibitors as a supplementary therapy for different types of tumor cells. Presently, ongoing research is being carried out to acquire an understanding of innovative and more efficacious methods for treating cancer. Continuing in this research approach, we aim to investigate the discovery, biosynthesis, mechanism of action, and biological features of geldanamycin and its analogs.https://qaaspa.com/index.php/bmtj/article/view/17cancergeldanamycinheat shock proteininhibitorshsp90 |
spellingShingle | Atta Mohammed Alzebari Amjad Mahmood Qadir Mahmood Sherzad Rafaat Abbas Salihi Therapeutic Potential of Heat Shock Protein 90 Inhibitors, Geldanamycin, and Analog Compounds in Precision Cancer Therapy BioMed Target Journal cancer geldanamycin heat shock protein inhibitors hsp90 |
title | Therapeutic Potential of Heat Shock Protein 90 Inhibitors, Geldanamycin, and Analog Compounds in Precision Cancer Therapy |
title_full | Therapeutic Potential of Heat Shock Protein 90 Inhibitors, Geldanamycin, and Analog Compounds in Precision Cancer Therapy |
title_fullStr | Therapeutic Potential of Heat Shock Protein 90 Inhibitors, Geldanamycin, and Analog Compounds in Precision Cancer Therapy |
title_full_unstemmed | Therapeutic Potential of Heat Shock Protein 90 Inhibitors, Geldanamycin, and Analog Compounds in Precision Cancer Therapy |
title_short | Therapeutic Potential of Heat Shock Protein 90 Inhibitors, Geldanamycin, and Analog Compounds in Precision Cancer Therapy |
title_sort | therapeutic potential of heat shock protein 90 inhibitors geldanamycin and analog compounds in precision cancer therapy |
topic | cancer geldanamycin heat shock protein inhibitors hsp90 |
url | https://qaaspa.com/index.php/bmtj/article/view/17 |
work_keys_str_mv | AT attamohammedalzebari therapeuticpotentialofheatshockprotein90inhibitorsgeldanamycinandanalogcompoundsinprecisioncancertherapy AT amjadmahmoodqadir therapeuticpotentialofheatshockprotein90inhibitorsgeldanamycinandanalogcompoundsinprecisioncancertherapy AT mahmoodsherzadrafaat therapeuticpotentialofheatshockprotein90inhibitorsgeldanamycinandanalogcompoundsinprecisioncancertherapy AT abbassalihi therapeuticpotentialofheatshockprotein90inhibitorsgeldanamycinandanalogcompoundsinprecisioncancertherapy |