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Article ; Online: The Challenges and Prospects of p53-Based Therapies in Ovarian Cancer.

Wallis, Bryce / Bowman, Katherine Redd / Lu, Phong / Lim, Carol S

2023 Volume 13, Issue 1

Abstract: It has been well established that mutations in the tumor suppressor gene, p53, occur readily in a vast majority of cancer tumors, including ovarian cancer. Typically diagnosed in stages three or four, ovarian cancer is the fifth leading cause of death in ...

Abstract	It has been well established that mutations in the tumor suppressor gene, p53, occur readily in a vast majority of cancer tumors, including ovarian cancer. Typically diagnosed in stages three or four, ovarian cancer is the fifth leading cause of death in women, despite accounting for only 2.5% of all female malignancies. The overall 5-year survival rate for ovarian cancer is around 47%; however, this drops to an abysmal 29% for the most common type of ovarian cancer, high-grade serous ovarian carcinoma (HGSOC). HGSOC has upwards of 96% of cases expressing mutations in p53. Therefore, wild-type (WT) p53 and p53-based therapies have been explored as treatment options via a plethora of drug delivery vehicles including nanoparticles, viruses, polymers, and liposomes. However, previous p53 therapeutics have faced many challenges, which have resulted in their limited translational success to date. This review highlights a selection of these historical p53-targeted therapeutics for ovarian cancer, why they failed, and what the future could hold for a new generation of this class of therapies.
MeSH term(s)	Female ; Humans ; Tumor Suppressor Protein p53/genetics ; Ovarian Neoplasms/drug therapy ; Ovarian Neoplasms/genetics ; Mutation
Chemical Substances	Tumor Suppressor Protein p53
Language	English
Publishing date	2023-01-12
Publishing country	Switzerland
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom13010159
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Article ; Online: Roadmap to affinity-tuned antibodies for enhanced chimeric antigen receptor T cell function and selectivity.

Vander Mause, Erica R / Atanackovic, Djordje / Lim, Carol S / Luetkens, Tim

Trends in biotechnology

2022 Volume 40, Issue 7, Page(s) 875–890

Abstract: Chimeric antigen receptor (CAR) T cells have revolutionized cancer treatment. CARs use antibody-derived binding domains to redirect T cells to antigens expressed on the surface of cancer cells. However, the high affinity of most currently used CAR- ... ...

Abstract	Chimeric antigen receptor (CAR) T cells have revolutionized cancer treatment. CARs use antibody-derived binding domains to redirect T cells to antigens expressed on the surface of cancer cells. However, the high affinity of most currently used CAR-binding domains results in excessive T-cell activation limiting CAR T-cell persistence and the inability to differentiate between antigen-high tumor cells and antigen-low healthy cells. We review recent data on the use of low-affinity CAR-binding domains and evaluate technologies and approaches to engineer and screen low-affinity antibody variants for CAR T-cell development. We propose an ideal workflow for the generation of optimal low-affinity binders derived from existing antibodies to streamline the development of more functional and selective therapeutics.
MeSH term(s)	Immunotherapy, Adoptive/methods ; Receptors, Chimeric Antigen/genetics ; Receptors, Chimeric Antigen/metabolism ; Signal Transduction ; T-Lymphocytes
Chemical Substances	Receptors, Chimeric Antigen
Language	English
Publishing date	2022-01-22
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	47474-5
ISSN	1879-3096 ; 0167-7799
ISSN (online)	1879-3096
ISSN	0167-7799
DOI	10.1016/j.tibtech.2021.12.009
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Article: Computational Modeling of Stapled Coiled-Coil Inhibitors Against Bcr-Abl: Toward a Treatment Strategy for CML.

Lima, Maria Carolina P / Hornsby, Braxten D / Lim, Carol S / Cheatham, Thomas E

bioRxiv : the preprint server for biology

2023

Abstract: The chimeric oncoprotein Bcr-Abl is the causative agent of virtually all chronic myeloid leukemias (CML) and a subset of acute lymphoblastic leukemias (ALL). As a result of the so-called Philadelphia Chromosome translocation t(9;22), Bcr-Abl manifests as ...

Abstract	The chimeric oncoprotein Bcr-Abl is the causative agent of virtually all chronic myeloid leukemias (CML) and a subset of acute lymphoblastic leukemias (ALL). As a result of the so-called Philadelphia Chromosome translocation t(9;22), Bcr-Abl manifests as a constitutively active tyrosine kinase which promotes leukemogenesis by activation of cell cycle signaling pathways. Constitutive and oncogenic activation is mediated by an N-terminal coiled-coil oligomerization domain in Bcr (Bcr-CC), presenting a therapeutic target for inhibition of Bcr-Abl activity toward the treatment of Bcr-Abl+ leukemias. Previously, we demonstrated that a rationally designed Bcr-CC mutant, CCmut3, exerts a dominant negative effect upon Bcr-Abl activity by preferential oligomerization with Bcr-CC. Moreover, we have shown conjugation to a leukemia-specific cell-penetrating peptide (CPP-CCmut3) improves intracellular delivery and activity. However, our full-length CPP-CCmut3 construct (81 aa) is encumbered by an intrinsically high degree of conformational variability and susceptibility to proteolytic degradation, relative to traditional small molecule therapeutics. Here, we iterate a new generation of our inhibitor against Bcr-CC mediated Bcr-Abl assembly that is designed to address these constraints through incorporation of all-hydrocarbon staples spanning i, i + 7 positions in helix α2 (CPP-CCmut3-st). We utilize computational modeling and biomolecular simulation to design and characterize single and double staple candidates in silico, evaluating binding energetics and building upon our seminal work modeling single hydrocarbon staples when applied to a truncated Bcr-CC sequence. This strategy enables us to efficiently build, characterize, and screen lead single/double stapled CPP-CCmut3-st candidates for experimental studies and validation in vitro and in vivo. In addition to full-length CPP-CCmut, we model a truncated system characterized by deletion of helix α1 and the flexible-loop linker, which are known to impart high conformational variability. To study the impact of the N-terminal cyclic CPP toward model stability and inhibitor activity, we also model the full-length and truncated systems without CPP, with cyclized CPP, and with linear CPP, for a total of six systems which comprise our library. From this library, we present lead stapled peptide candidates to be synthesized and evaluated experimentally as our next-generation inhibitors against Bcr-Abl.
Language	English
Publishing date	2023-11-17
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.11.15.566894
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Article: Roadmap to affinity-tuned antibodies for enhanced chimeric antigen receptor T cell function and selectivity

Vander Mause, Erica R. / Atanackovic, Djordje / Lim, Carol S. / Luetkens, Tim

Trends in biotechnology. 2021,

2021

Abstract	Chimeric antigen receptor (CAR) T cells have revolutionized cancer treatment. CARs use antibody-derived binding domains to redirect T cells to antigens expressed on the surface of cancer cells. However, the high affinity of most currently used CAR-binding domains results in excessive T-cell activation limiting CAR T-cell persistence and the inability to differentiate between antigen-high tumor cells and antigen-low healthy cells. We review recent data on the use of low-affinity CAR-binding domains and evaluate technologies and approaches to engineer and screen low-affinity antibody variants for CAR T-cell development. We propose an ideal workflow for the generation of optimal low-affinity binders derived from existing antibodies to streamline the development of more functional and selective therapeutics.
Keywords	T-lymphocytes ; antibodies ; antigens ; biotechnology ; cancer therapy ; neoplasms
Language	English
Publishing place	Elsevier Ltd
Document type	Article
Note	Pre-press version
ZDB-ID	47474-5
ISSN	1879-3096 ; 0167-7799
ISSN (online)	1879-3096
ISSN	0167-7799
DOI	10.1016/j.tibtech.2021.12.009
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Article ; Online: Narrowing the field: cancer-specific promoters for mitochondrially-targeted p53-BH3 fusion gene therapy in ovarian cancer.

Bowman, Katherine Redd / Kim, Ji Hoon / Lim, Carol S

Journal of ovarian research

2019 Volume 12, Issue 1, Page(s) 38

Abstract: Background: Despite years of research, the treatment options and mortality rate for ovarian cancer remain relatively stagnant. Resistance to chemotherapy and high heterogeneity in mutations contribute to ovarian cancer's lethality, including many ... ...

Abstract	Background: Despite years of research, the treatment options and mortality rate for ovarian cancer remain relatively stagnant. Resistance to chemotherapy and high heterogeneity in mutations contribute to ovarian cancer's lethality, including many mutations in tumor suppressor p53. Though wild type p53 gene therapy clinical trials failed in ovarian cancer, mitochondrially-targeted p53 fusion constructs, including a fusion with pro-apoptotic protein Bad, have shown much higher apoptotic potential than wild type p53 in vitro. Due to the inherent toxicities of mitochondrial apoptosis, cancer-specificity for the p53 fusion constructs must be developed. Cancer-specific promoters such as hTERT, hTC, Brms1, and Ran have shown promise in ovarian cancer. Results: Of five different lengths of hTERT promoter, the - 279/+ 5 length relative to the transcription start site showed the highest activity across a panel of ovarian cancer cells. In addition to - 279/+ 5, promoters hTC (an hTERT/CMV promoter hybrid), Brms1, and Ran were tested as drivers of mitochondrially-targeted p53-Bad and p53-Bad* fusion gene therapy constructs. p53-Bad* displayed cancer-specific killing in all ovarian cancer cell lines when driven by hTC, - 279/+ 5, or Brms1. Conclusions: Cancer-specific promoters hTC, - 279/+ 5, and Brms1 all display promise in driving p53-Bad* gene therapy for treatment of ovarian cancer and should be moved forward into in vivo studies. -279/+ 5 displays lower expression levels in fewer cells, but greater cancer specificity, rendering it most useful for gene therapeutics with high toxicity to normal cells. hTC and Brms1 show higher transfection and expression levels with some cancer specificity, making them ideal for lowering toxicity in order to increase dose without as much of a reduction in the number of cancer cells expressing the gene construct. Having a variety of promoters available means that patient genetic testing can aid in choosing a promoter, thereby increasing cancer-specificity and giving patients with ovarian cancer a greater chance at survival.
MeSH term(s)	Female ; Genetic Therapy/methods ; Humans ; Ovarian Neoplasms/genetics ; Ovarian Neoplasms/pathology ; Promoter Regions, Genetic/genetics ; Transfection ; Tumor Suppressor Protein p53/genetics
Chemical Substances	Tumor Suppressor Protein p53
Language	English
Publishing date	2019-04-30
Publishing country	England
Document type	Journal Article
ZDB-ID	2455679-8
ISSN	1757-2215 ; 1757-2215
ISSN (online)	1757-2215
ISSN	1757-2215
DOI	10.1186/s13048-019-0514-4
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Article ; Online: Inhibition of bcr-abl in human leukemic cells with a coiled-coil protein delivered by a leukemia-specific cell-penetrating Peptide.

Bruno, Benjamin J / Lim, Carol S

Molecular pharmaceutics

2015 Volume 12, Issue 5, Page(s) 1412–1421

Abstract: The oncoprotein Bcr-Abl is the cause of chronic myeloid leukemia (CML).1 Current therapies target the tyrosine kinase domain of Bcr-Abl, but resistance to these drugs is common.2 Bcr-Abl homo-oligomerization via its N-terminal coiled-coil (CC) domain is ... ...

Abstract	The oncoprotein Bcr-Abl is the cause of chronic myeloid leukemia (CML).1 Current therapies target the tyrosine kinase domain of Bcr-Abl, but resistance to these drugs is common.2 Bcr-Abl homo-oligomerization via its N-terminal coiled-coil (CC) domain is required for tyrosine kinase activity.3 Our previous work has shown that it is possible to inhibit Bcr-Abl activity by targeting the CC domain with a peptidomemetic known as CC(mut3), delivered as a plasmid.4 In this study, CC(mut3) is delivered to cells as a protein by utilizing a leukemia-specific cell-penetrating peptide (CPP).5 Here, recombinant CPP-CC(mut3) was expressed, purified, and tested for its antioncogenic activity. CPP-CC(mut3) was able to enter two leukemic cell lines (K562 and Ba/F3-P210) and inhibit Bcr-Abl activity as shown by induction of necrosis/apoptosis via 7-AAD/Annexin V staining, reduction of oncogenic potential in colony forming assays, reduction of cell proliferation, and inhibition of Bcr-Abl phosphorylation (kinase activity). Further, CPP-CC(mut3) did not enter nonleukemic cell lines (HEK293 and MCF-7). While CPP-CC(mut3) was able to enter the parental, nonleukemic Bcr-Abl(-) Ba/F3 pro-B cell line, it revealed no signs of activity in the assays performed, as expected. These results indicate the feasibility of using CPP-CC(mut3) as a therapeutic against CML.
MeSH term(s)	Annexin A5/metabolism ; Apoptosis/drug effects ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Cell-Penetrating Peptides/chemistry ; Cell-Penetrating Peptides/pharmacology ; Enzyme Activation/drug effects ; Fusion Proteins, bcr-abl/metabolism ; HEK293 Cells ; Humans ; K562 Cells ; Necrosis/chemically induced ; Phosphorylation/drug effects ; Protein Structure, Tertiary ; Spectrometry, Mass, Electrospray Ionization ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chemical Substances	Annexin A5 ; Cell-Penetrating Peptides ; Fusion Proteins, bcr-abl (EC 2.7.10.2)
Language	English
Publishing date	2015-05-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2138405-8
ISSN	1543-8392 ; 1543-8384
ISSN (online)	1543-8392
ISSN	1543-8384
DOI	10.1021/mp500701u
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Article: Mapping the Evidence for Opioid-Mediated Changes in Malignancy and Chemotherapeutic Efficacy: Protocol for a Scoping Review.

Constance, Jonathan E / McFarland, Mary M / Casucci, Tallie / Deininger, Michael W / Enioutina, Elena Y / Job, Kathleen / Lemons, Richard S / Lim, Carol S / Ward, Robert M / Yellepeddi, Venkata / Watt, Kevin M

JMIR research protocols

2023 Volume 12, Page(s) e38167

Abstract: Background: Numerous reports contend opioids can augment or inhibit malignancy. At present, there is no consensus on the risk or benefit posed by opioids on malignancy or chemotherapeutic activity. Distinguishing the consequences of opioid use from pain ...

Abstract	Background: Numerous reports contend opioids can augment or inhibit malignancy. At present, there is no consensus on the risk or benefit posed by opioids on malignancy or chemotherapeutic activity. Distinguishing the consequences of opioid use from pain and its management is challenging. Additionally, opioid concentration data is often lacking in clinical studies. A scoping review approach inclusive of preclinical and clinical data will improve our understanding of the risk-benefit relationship concerning commonly prescribed opioids and cancer and cancer treatment. Objective: The aim of the study is to map diverse studies spanning from preclinical to clinical regarding opioids with malignancy and its treatment. Methods: This scoping review will use the Arksey six stages framework to (1) identify the research question; (2) identify relevant studies; (3) select studies meeting criteria; (4) extract and chart data; (5) collate, summarize, and report results; and (6) conduct expert consultation. An initial pilot study was undertaken to (1) parameterize the extent and scale of existing data for an evidence review, (2) identify key factors to be extracted in systematic charting efforts, and (3) assess opioid concentration as a variable for its relevance to the central hypothesis. Six databases will be searched with no filters: MEDLINE, Embase, CINAHL Complete, Cochrane Library, Biological Sciences Collection, and International Pharmaceutical Abstracts. Trial registries will include ClinicalTrials.gov, Cochrane CENTRAL, International Standard Randomised Controlled Trial Number Registry, European Union Clinical Trials Register, and World Health Organization International Clinical Trials Registry. Eligibility criteria will include preclinical and clinical study data on opioids effects on tumor growth or survival, or alteration on the antineoplastic activity of chemotherapeutics. We will chart data on (1) opioid concentration from human subjects with cancer, yielding a "physiologic range" to better interpret available preclinical data; (2) patterns of opioid exposure with disease and treatment-related patient outcomes; and (3) the influence of opioids on cancer cell survival, as well as opioid-related changes to cancer cell susceptibility for chemotherapeutics. Results: This scoping review will present results in narrative forms as well as with the use of tables and diagrams. Initiated in February 2021 at the University of Utah, this protocol is anticipated to generate a scoping review by August 2023. The results of the scoping review will be disseminated through scientific conference proceedings and presentations, stakeholder meetings, and by publication in a peer-reviewed journal. Conclusions: The findings of this scoping review will provide a comprehensive description of the consequences of prescription opioids on malignancy and its treatment. By incorporating preclinical and clinical data, this scoping review will invite novel comparisons across study types that could inform new basic, translational, and clinical studies regarding risks and benefits of opioid use among patients with cancer. International registered report identifier (irrid): PRR1-10.2196/38167.
Language	English
Publishing date	2023-05-22
Publishing country	Canada
Document type	Journal Article
ZDB-ID	2719222-2
ISSN	1929-0748
ISSN	1929-0748
DOI	10.2196/38167
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Article ; Online: Computational Modeling of Stapled Peptides toward a Treatment Strategy for CML and Broader Implications in the Design of Lengthy Peptide Therapeutics.

Cornillie, Sean P / Bruno, Benjamin J / Lim, Carol S / Cheatham, Thomas E

The journal of physical chemistry. B

2018 Volume 122, Issue 14, Page(s) 3864–3875

Abstract: The oncogenic gene product Bcr-Abl is the principal cause of chronic myeloid leukemia, and although several therapies exist to curb the aberrant kinase activity of Bcr-Abl through targeting of the Abl kinase domain, these therapies are rendered ... ...

Abstract	The oncogenic gene product Bcr-Abl is the principal cause of chronic myeloid leukemia, and although several therapies exist to curb the aberrant kinase activity of Bcr-Abl through targeting of the Abl kinase domain, these therapies are rendered ineffective by frequent mutations in the corresponding gene. It has been demonstrated that a designed protein, known as CCmut3, is able to produce a dominant negative inactivating effect on Bcr-Abl kinase by preferentially oligomerizing with the N-terminal coiled-coil oligomerization domain of Bcr-Abl (Bcr-CC) to effectively reduce the oncogenic potential of Bcr-Abl. However, the sheer length of the CCmut3 peptide introduces a high degree of conformational variability and opportunity for targeting by intracellular proteolytic mechanisms. Here, we have examined the effects of introducing one or two molecular staples, or cross-links, spanning i, i + 7 backbone residues of the CCmut3 construct, which have been suggested to reinforce α-helical conformation, enhance cellular internalization, and increase resistance to proteolytic degradation, leading to enhanced pharmacokinetic properties. The importance of optimizing staple location along a highly tuned biological construct such as CCmut3 has been widely emphasized and, as such, we have employed in silico techniques to swiftly build, relax, and characterize a large number of candidates. This approach effectively allowed exploring each and every possible staple location along the peptide backbone so that every possible candidate is considered. Although many of the stapled candidate peptides displayed enhanced binding characteristics for Bcr-CC and improved conformational stability in the (Bcr-CC) bound form, simulations of the stapled peptides in the unbound form revealed widespread conformational variability among stapled candidates dependent on staple type and location, implicating the molecular replacement of helix-stabilizing residues with staple-containing residues in disrupting the native α-helical conformation of CCmut3, further highlighting a need for careful optimization of the CCmut3 construct. A candidate set has been assembled, which retains the native backbone α-helical integrity in both the bound and unbound forms while providing enhanced binding affinity for the Bcr-CC target, as research disseminated in this manuscript is intended to guide the development of a next-generation CCmut3 inhibitor peptide in an experimental setting.
MeSH term(s)	Drug Design ; Humans ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/drug therapy ; Molecular Conformation ; Molecular Dynamics Simulation ; Peptides/chemical synthesis ; Peptides/chemistry ; Peptides/therapeutic use
Chemical Substances	Peptides
Language	English
Publishing date	2018--12
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1520-5207
ISSN (online)	1520-5207
DOI	10.1021/acs.jpcb.8b01014
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Article ; Online: Advances in delivery vectors for gene therapy in liver cancer.

Redd Bowman, Katherine E / Lu, Phong / Vander Mause, Erica R / Lim, Carol S

Therapeutic delivery

2019 Volume 11, Issue 1, Page(s) 833–850

Abstract: Hepatocellular carcinoma (HCC) is the third most common cause of cancer death globally, mainly due to lack of effective treatments - a problem that gene therapy is poised to solve. Successful gene therapy requires safe and efficient delivery vectors, and ...

Abstract	Hepatocellular carcinoma (HCC) is the third most common cause of cancer death globally, mainly due to lack of effective treatments - a problem that gene therapy is poised to solve. Successful gene therapy requires safe and efficient delivery vectors, and recent advances in both viral and nonviral vectors have made an important impact on HCC gene therapy delivery. This review explores how adenoviral, retroviral and adeno-associated viral vectors have been modified to increase safety and delivery capacity, highlighting studies and clinical trials using these vectors for HCC gene therapy. Nanoparticles, liposomes, exosomes and virosomes are also featured in their roles as HCC gene delivery vectors. Finally, new discoveries in gene editing technology and their impacts on HCC gene therapy are discussed.
MeSH term(s)	Carcinoma, Hepatocellular/genetics ; Carcinoma, Hepatocellular/therapy ; Gene Transfer Techniques ; Genetic Therapy ; Genetic Vectors ; Humans ; Liver Neoplasms/genetics ; Liver Neoplasms/therapy
Language	English
Publishing date	2019-12-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	2041-6008
ISSN (online)	2041-6008
DOI	10.4155/tde-2019-0076
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Article: Targeting malignant mitochondria with therapeutic peptides.

Constance, Jonathan E / Lim, Carol S

Therapeutic delivery

2012 Volume 3, Issue 8, Page(s) 961–979

Abstract: The current status of peptides that target the mitochondria in the context of cancer is the focus of this review. Chemotherapy and radiotherapy used to kill tumor cells are principally mediated by the process of apoptosis that is governed by the ... ...

Abstract	The current status of peptides that target the mitochondria in the context of cancer is the focus of this review. Chemotherapy and radiotherapy used to kill tumor cells are principally mediated by the process of apoptosis that is governed by the mitochondria. The failure of anticancer therapy often resides at the level of the mitochondria. Therefore, the mitochondrion is a key pharmacological target in cancer due to many of the differences that arise between malignant and healthy cells at the level of this ubiquitous organelle. Additionally, targeting the characteristics of malignant mitochondira often rely on disruption of protein--protein interactions that are not generally amenable to small molecules. We discuss anticancer peptides that intersect with pathological changes in the mitochondrion.
MeSH term(s)	Antineoplastic Agents/administration & dosage ; Antineoplastic Agents/therapeutic use ; Apoptosis/drug effects ; Drug Delivery Systems/methods ; Humans ; Mitochondria/drug effects ; Mitochondria/metabolism ; Models, Biological ; Neoplasms/drug therapy ; Peptides/administration & dosage ; Peptides/therapeutic use ; Signal Transduction/drug effects
Chemical Substances	Antineoplastic Agents ; Peptides
Language	English
Publishing date	2012-09-03
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ISSN	2041-5990
ISSN	2041-5990
DOI	10.4155/tde.12.75
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