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Article ; Online: Structures of Hsp90α and Hsp90β bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivity.

Huck, John D / Que, Nanette L S / Sharma, Sahil / Taldone, Tony / Chiosis, Gabriela / Gewirth, Daniel T

2019 Volume 87, Issue 10, Page(s) 869–877

Abstract: Hsp90α and Hsp90β are implicated in a number of cancers and neurodegenerative disorders but the lack of selective pharmacological probes confounds efforts to identify their individual roles. Here, we analyzed the binding of an Hsp90α-selective PU ... ...

Abstract	Hsp90α and Hsp90β are implicated in a number of cancers and neurodegenerative disorders but the lack of selective pharmacological probes confounds efforts to identify their individual roles. Here, we analyzed the binding of an Hsp90α-selective PU compound, PU-11-trans, to the two cytosolic paralogs. We determined the co-crystal structures of Hsp90α and Hsp90β bound to PU-11-trans, as well as the structure of the apo Hsp90β NTD. The two inhibitor-bound structures reveal that Ser52, a nonconserved residue in the ATP binding pocket in Hsp90α, provides additional stability to PU-11-trans through a water-mediated hydrogen-bonding network. Mutation of Ser52 to alanine, as found in Hsp90β, alters the dissociation constant of Hsp90α for PU-11-trans to match that of Hsp90β. Our results provide a structural explanation for the binding preference of PU inhibitors for Hsp90α and demonstrate that the single nonconserved residue in the ATP-binding pocket may be exploited for α/β selectivity.
MeSH term(s)	Amino Acid Sequence ; Amino Acids/chemistry ; Amino Acids/genetics ; Amino Acids/metabolism ; Drug Development ; Drug Discovery ; HSP90 Heat-Shock Proteins/antagonists & inhibitors ; HSP90 Heat-Shock Proteins/chemistry ; HSP90 Heat-Shock Proteins/genetics ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Mutation ; Protein Conformation ; Purines/chemistry ; Purines/metabolism ; Sequence Homology
Chemical Substances	Amino Acids ; HSP90 Heat-Shock Proteins ; HSP90AA2P protein, human ; HSP90AB1 protein, human ; Purines
Language	English
Publishing date	2019-06-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	806683-8
ISSN	1097-0134 ; 0887-3585
ISSN (online)	1097-0134
ISSN	0887-3585
DOI	10.1002/prot.25750
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Article ; Online: Chemical probes and methods for single-cell detection and quantification of epichaperomes in hematologic malignancies.

Merugu, Swathi / Sharma, Sahil / Kaner, Justin / Digwal, Chander / Sugita, Mayumi / Joshi, Suhasini / Taldone, Tony / Guzman, Monica L / Chiosis, Gabriela

Methods in enzymology

2020 Volume 639, Page(s) 289–311

Abstract: Detection of protein connectivity dysfunctions in biological samples, i.e., informing on how protein-protein interactions change from a normal to a disease state, is important for both biomedical research and clinical development. The epichaperome is an ... ...

Abstract	Detection of protein connectivity dysfunctions in biological samples, i.e., informing on how protein-protein interactions change from a normal to a disease state, is important for both biomedical research and clinical development. The epichaperome is an executor of protein connectivity dysfunction in disease, and thus a surrogate for its detection. This chapter will detail on published methods for epichaperome detection and quantification that combine the advantages of multiparameter flow cytometry with those of the PU-FITC fluorescently labeled epichaperome detection probe. It will offer a comprehensive method description that includes the synthesis and characterization of an epichaperome detection probe and of the negative control probe, the preparation of the biospecimen for epichaperome analysis, the execution of the epichaperome detection and quantification assay and lastly, the data acquisition and analysis. The method provides, at single-cell level, the functional signature of cells, differentiating itself from other single-cell methods that provide a catalog of molecules.
MeSH term(s)	Flow Cytometry ; Hematologic Neoplasms ; Humans
Language	English
Publishing date	2020-05-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1557-7988
ISSN (online)	1557-7988
DOI	10.1016/bs.mie.2020.04.057
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Article ; Online: Heat Shock Protein (HSP) Drug Discovery and Development: Targeting Heat Shock Proteins in Disease.

Shrestha, Liza / Bolaender, Alexander / Patel, Hardik J / Taldone, Tony

Current topics in medicinal chemistry

2016 Volume 16, Issue 25, Page(s) 2753–2764

Abstract: Heat shock proteins (HSPs) present as a double edged sword. While they play an important role in maintaining protein homeostasis in a normal cell, cancer cells have evolved to co-opt HSP function to promote their own survival. As a result, HSPs such as ... ...

Abstract	Heat shock proteins (HSPs) present as a double edged sword. While they play an important role in maintaining protein homeostasis in a normal cell, cancer cells have evolved to co-opt HSP function to promote their own survival. As a result, HSPs such as HSP90 have attracted a great deal of interest as a potential anticancer target. These efforts have resulted in over 20 distinct compounds entering clinical evaluation for the treatment of cancer. However, despite the potent anticancer activity demonstrated in preclinical models, to date no HSP90 inhibitor has obtained regulatory approval. In this review we discuss the unique challenges faced in targeting HSPs that have likely contributed to their lack of progress in the clinic and suggest ways to overcome these so that the enormous potential of these compounds to benefit patients can finally be realized. We also provide a guideline for the future development of HSP-targeted agents based on the many lessons learned during the last two decades in developing HSP90 inhibitors.
MeSH term(s)	Antineoplastic Agents/pharmacology ; Drug Discovery ; Heat-Shock Proteins/antagonists & inhibitors ; Heat-Shock Proteins/metabolism ; Humans ; Protein Binding
Chemical Substances	Antineoplastic Agents ; Heat-Shock Proteins
Language	English
Publishing date	2016-04-12
Publishing country	United Arab Emirates
Document type	Journal Article ; Review
ZDB-ID	2064823-6
ISSN	1873-4294 ; 1568-0266
ISSN (online)	1873-4294
ISSN	1568-0266
DOI	10.2174/1568026616666160413141911
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Zs.A 5572: Show issues

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Article: Copper Mediated Coupling of 2-(Piperazine)-pyrimidine Iodides with Aryl Thiols using Cu(I)Thiophene-2-carboxylate.

Shrestha, Liza / Patel, Hardik J / Kang, Yanlong / Sharma, Sahil / Chiosis, Gabriela / Taldone, Tony

Tetrahedron letters

2017 Volume 58, Issue 48, Page(s) 4525–4531

Abstract: A copper-mediated synthesis of diaryl sulfides utilizing Cu(I)-thiophene-2-carboxylate (CuTC) is described. We demonstrate the use of CuTC as a soluble, non-basic catalyst in the coupling of aryl iodides and aryl thiols in the synthesis of synthetically ... ...

Abstract	A copper-mediated synthesis of diaryl sulfides utilizing Cu(I)-thiophene-2-carboxylate (CuTC) is described. We demonstrate the use of CuTC as a soluble, non-basic catalyst in the coupling of aryl iodides and aryl thiols in the synthesis of synthetically advanced diaryl sulfides. This method allows for the successful coupling of challenging substrates including
Language	English
Publishing date	2017-10-23
Publishing country	England
Document type	Journal Article
ZDB-ID	204287-3
ISSN	1873-3581 ; 0040-4039
ISSN (online)	1873-3581
ISSN	0040-4039
DOI	10.1016/j.tetlet.2017.10.041
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Zs.A 2837: Show issues

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Article ; Online: NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90.

Huck, John D / Que, Nanette L S / Immormino, Robert M / Shrestha, Liza / Taldone, Tony / Chiosis, Gabriela / Gewirth, Daniel T

The Journal of biological chemistry

2019 Volume 294, Issue 44, Page(s) 16010–16019

Abstract: The hsp90 chaperones govern the function of essential client proteins critical for normal cell function as well as cancer initiation and progression. Hsp90 activity is driven by ATP, which binds to the N-terminal domain and induces large conformational ... ...

Abstract	The hsp90 chaperones govern the function of essential client proteins critical for normal cell function as well as cancer initiation and progression. Hsp90 activity is driven by ATP, which binds to the N-terminal domain and induces large conformational changes that are required for client maturation. Inhibitors targeting the ATP-binding pocket of the N-terminal domain have anticancer effects, but most bind with similar affinity to cytosolic Hsp90α and Hsp90β, endoplasmic reticulum Grp94, and mitochondrial Trap1, the four cellular hsp90 paralogs. Paralog-specific inhibitors may lead to drugs with fewer side effects. The ATP-binding pockets of the four paralogs are flanked by three side pockets, termed sites 1, 2, and 3, which differ between the paralogs in their accessibility to inhibitors. Previous insights into the principles governing access to sites 1 and 2 have resulted in development of paralog-selective inhibitors targeting these sites, but the rules for selective targeting of site 3 are less clear. Earlier studies identified 5'
MeSH term(s)	Adenosine-5'-(N-ethylcarboxamide)/analogs & derivatives ; Adenosine-5'-(N-ethylcarboxamide)/pharmacology ; Allosteric Regulation ; Binding Sites ; Humans ; Membrane Glycoproteins/chemistry ; Membrane Glycoproteins/metabolism ; Molecular Docking Simulation ; Protein Binding
Chemical Substances	Membrane Glycoproteins ; endoplasmin ; Adenosine-5'-(N-ethylcarboxamide) (35920-39-9)
Language	English
Publishing date	2019-09-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA119.009960
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Article ; Online: Purine-scaffold Hsp90 inhibitors.

Taldone, Tony / Chiosis, Gabriela

Current topics in medicinal chemistry

2009 Volume 9, Issue 15, Page(s) 1436–1446

Abstract: Hsp90 is a molecular chaperone with important roles in regulating the function of several proteins with potential pathogenic activity. Because many of these proteins are involved in cancer and neurodegenerative promoting pathways, Hsp90 has emerged as an ...

Abstract	Hsp90 is a molecular chaperone with important roles in regulating the function of several proteins with potential pathogenic activity. Because many of these proteins are involved in cancer and neurodegenerative promoting pathways, Hsp90 has emerged as an attractive therapeutic target in these diseases. Molecules that bind to the N-terminal nucleotide pocket of Hsp90 inhibit its activity, and consequently, disrupt client protein function. A number of these inhibitors from several chemical classes are now known, and some are already in clinical trials. This review focuses on the purine class of Hsp90 inhibitors, their discovery through rational design, and on efforts aimed towards their optimization and development into clinically viable drugs for the treatment of cancer. Their potential towards neurodegenerative diseases will also be touched upon.
MeSH term(s)	Animals ; Drug Design ; HSP90 Heat-Shock Proteins/antagonists & inhibitors ; HSP90 Heat-Shock Proteins/chemistry ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Purines/chemical synthesis ; Purines/chemistry ; Purines/pharmacology ; Structure-Activity Relationship
Chemical Substances	HSP90 Heat-Shock Proteins ; Purines
Language	English
Publishing date	2009-05-16
Publishing country	United Arab Emirates
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2064823-6
ISSN	1873-4294 ; 1568-0266
ISSN (online)	1873-4294
ISSN	1568-0266
DOI	10.2174/156802609789895737
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Zs.A 5572: Show issues

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Article ; Online: Selective targeting of the stress chaperome as a therapeutic strategy.

Taldone, Tony / Ochiana, Stefan O / Patel, Pallav D / Chiosis, Gabriela

Trends in pharmacological sciences

2014 Volume 35, Issue 11, Page(s) 592–603

Abstract: Normal cellular function is maintained by coordinated proteome machinery that performs a vast array of activities. Helping the proteome in such roles is the chaperome, a network of molecular chaperones and folding enzymes. The stressed cell contains, at ... ...

Abstract	Normal cellular function is maintained by coordinated proteome machinery that performs a vast array of activities. Helping the proteome in such roles is the chaperome, a network of molecular chaperones and folding enzymes. The stressed cell contains, at any time, a complex mixture of chaperome complexes; a majority performs 'housekeeping functions' similarly to non-stressed, normal cells, but a finely-tuned fraction buffers the proteome altered by chronic stress. The stress chaperome is epigenetically distinct from its normal, housekeeping counterpart, providing a basis for its selective targeting by small molecules. We discuss here the development of chaperome inhibitors, and how agents targeting chaperome members in stressed cells are in fact being directed towards chaperome complexes, and their effect is therefore determined by their ability to sample and engage such complexes. A new approach is needed to target and implement chaperome modulators in the investigation of diseases, and we propose that the classical thinking in drug discovery needs adjustment when developing chaperome-targeting drugs.
MeSH term(s)	Animals ; Heat-Shock Proteins/antagonists & inhibitors ; Heat-Shock Proteins/chemistry ; Heat-Shock Proteins/metabolism ; Humans ; Models, Molecular ; Molecular Chaperones/antagonists & inhibitors ; Molecular Chaperones/chemistry ; Molecular Chaperones/metabolism ; Molecular Targeted Therapy
Chemical Substances	Heat-Shock Proteins ; Molecular Chaperones
Language	English
Publishing date	2014-09-25
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	282846-7
ISSN	1873-3735 ; 0165-6147
ISSN (online)	1873-3735
ISSN	0165-6147
DOI	10.1016/j.tips.2014.09.001
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Zs.A 1513: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 6: Show issues

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Article ; Online: A Chemical Biology Approach to the Chaperome in Cancer-HSP90 and Beyond.

Taldone, Tony / Wang, Tai / Rodina, Anna / Pillarsetty, Naga Vara Kishore / Digwal, Chander S / Sharma, Sahil / Yan, Pengrong / Joshi, Suhasini / Pagare, Piyusha P / Bolaender, Alexander / Roboz, Gail J / Guzman, Monica L / Chiosis, Gabriela

Cold Spring Harbor perspectives in biology

2020 Volume 12, Issue 4

Abstract: Cancer is often associated with alterations in the chaperome, a collection of chaperones, cochaperones, and other cofactors. Changes in the expression levels of components of the chaperome, in the interaction strength among chaperome components, ... ...

Abstract	Cancer is often associated with alterations in the chaperome, a collection of chaperones, cochaperones, and other cofactors. Changes in the expression levels of components of the chaperome, in the interaction strength among chaperome components, alterations in chaperome constituency, and in the cellular location of chaperome members, are all hallmarks of cancer. Here we aim to provide an overview on how chemical biology has played a role in deciphering such complexity in the biology of the chaperome in cancer and in other diseases. The focus here is narrow and on pathologic changes in the chaperome executed by enhancing the interaction strength between components of distinct chaperome pathways, specifically between those of HSP90 and HSP70 pathways. We will review chemical tools and chemical probe-based assays, with a focus on HSP90. We will discuss how kinetic binding, not classical equilibrium binding, is most appropriate in the development of drugs and probes for the chaperome in disease. We will then present our view on how chaperome inhibitors may become potential drugs and diagnostics in cancer.
MeSH term(s)	Animals ; Antineoplastic Agents/pharmacology ; Biology ; Decision Making ; Drug Design ; Gene Expression Regulation, Neoplastic ; HEK293 Cells ; HSP70 Heat-Shock Proteins/metabolism ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; K562 Cells ; Kinetics ; Mice ; Molecular Chaperones/metabolism ; NIH 3T3 Cells ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Protein Binding
Chemical Substances	Antineoplastic Agents ; HSP70 Heat-Shock Proteins ; HSP90 Heat-Shock Proteins ; Molecular Chaperones
Language	English
Publishing date	2020-04-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ISSN	1943-0264
ISSN (online)	1943-0264
DOI	10.1101/cshperspect.a034116
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Article ; Online: Systems-level analyses of protein-protein interaction network dysfunctions via epichaperomics identify cancer-specific mechanisms of stress adaptation.

Rodina, Anna / Xu, Chao / Digwal, Chander S / Joshi, Suhasini / Patel, Yogita / Santhaseela, Anand R / Bay, Sadik / Merugu, Swathi / Alam, Aftab / Yan, Pengrong / Yang, Chenghua / Roychowdhury, Tanaya / Panchal, Palak / Shrestha, Liza / Kang, Yanlong / Sharma, Sahil / Almodovar, Justina / Corben, Adriana / Alpaugh, Mary L /

Modi, Shanu / Guzman, Monica L / Fei, Teng / Taldone, Tony / Ginsberg, Stephen D / Erdjument-Bromage, Hediye / Neubert, Thomas A / Manova-Todorova, Katia / Tsou, Meng-Fu Bryan / Young, Jason C / Wang, Tai / Chiosis, Gabriela

Nature communications

2023 Volume 14, Issue 1, Page(s) 3742

Abstract: Systems-level assessments of protein-protein interaction (PPI) network dysfunctions are currently out-of-reach because approaches enabling proteome-wide identification, analysis, and modulation of context-specific PPI changes in native (unengineered) ... ...

Abstract	Systems-level assessments of protein-protein interaction (PPI) network dysfunctions are currently out-of-reach because approaches enabling proteome-wide identification, analysis, and modulation of context-specific PPI changes in native (unengineered) cells and tissues are lacking. Herein, we take advantage of chemical binders of maladaptive scaffolding structures termed epichaperomes and develop an epichaperome-based 'omics platform, epichaperomics, to identify PPI alterations in disease. We provide multiple lines of evidence, at both biochemical and functional levels, demonstrating the importance of these probes to identify and study PPI network dysfunctions and provide mechanistically and therapeutically relevant proteome-wide insights. As proof-of-principle, we derive systems-level insight into PPI dysfunctions of cancer cells which enabled the discovery of a context-dependent mechanism by which cancer cells enhance the fitness of mitotic protein networks. Importantly, our systems levels analyses support the use of epichaperome chemical binders as therapeutic strategies aimed at normalizing PPI networks.
MeSH term(s)	Humans ; Protein Interaction Maps ; Proteome/metabolism ; Protein Interaction Mapping ; Neoplasms/genetics ; Acclimatization
Chemical Substances	Proteome
Language	English
Publishing date	2023-06-23
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-39241-7
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Article: Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers.

Jhaveri, Komal / Taldone, Tony / Modi, Shanu / Chiosis, Gabriela

Biochimica et biophysica acta

2011 Volume 1823, Issue 3, Page(s) 742–755

Abstract: Hsp90 is an ATP dependent molecular chaperone protein which integrates multiple oncogenic pathways. As such, Hsp90 inhibition is a promising anti-cancer strategy. Several inhibitors that act on Hsp90 by binding to its N-terminal ATP pocket have entered ... ...

Abstract	Hsp90 is an ATP dependent molecular chaperone protein which integrates multiple oncogenic pathways. As such, Hsp90 inhibition is a promising anti-cancer strategy. Several inhibitors that act on Hsp90 by binding to its N-terminal ATP pocket have entered clinical evaluation. Robust pre-clinical data suggested anti-tumor activity in multiple cancer types. Clinically, encouraging results have been demonstrated in melanoma, acute myeloid leukemia, castrate refractory prostate cancer, non-small cell lung carcinoma and multiple myeloma. In breast cancer, proof-of-concept was demonstrated by first generation Hsp90 inhibitors in combination with trastuzumab mainly in human epidermal growth factor receptor 2 (HER2)+metastatic breast cancer. There are a multitude of second generation Hsp90 inhibitors currently under investigation. To date, however, there is no FDA approved Hsp90 inhibitor nor standardized assay to ascertain Hsp90 inhibition. This review summarizes the current status of both first and second generation Hsp90 inhibitors based on their chemical classification and stage of clinical development. It also discusses the pharmacodynamic assays currently implemented in clinic as well as other novel strategies aimed at enhancing the effectiveness of Hsp90 inhibitors. Ultimately, these efforts will aid in maximizing the full potential of this class of agents. This article is part of a Special Issue entitled: Heat Shock Protein 90 (HSP90).
MeSH term(s)	Antineoplastic Agents/pharmacology ; Clinical Trials as Topic ; HSP90 Heat-Shock Proteins/antagonists & inhibitors ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Neoplasms/drug therapy ; Neoplasms/metabolism
Chemical Substances	Antineoplastic Agents ; HSP90 Heat-Shock Proteins
Language	English
Publishing date	2011-10-29
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2011.10.008
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