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Article ; Online: Cancer Vaccines, Treatment of the Future: With Emphasis on HER2-Positive Breast Cancer.

Pallerla, Sandeep / Abdul, Ata Ur Rahman Mohammed / Comeau, Jill / Jois, Seetharama

International journal of molecular sciences

2021 Volume 22, Issue 2

Abstract: Breast cancer is one of the leading causes of death in women. With improvements in early-stage diagnosis and targeted therapies, there has been an improvement in the overall survival rate in breast cancer over the past decade. Despite the development of ... ...

Abstract	Breast cancer is one of the leading causes of death in women. With improvements in early-stage diagnosis and targeted therapies, there has been an improvement in the overall survival rate in breast cancer over the past decade. Despite the development of targeted therapies, tyrosine kinase inhibitors, as well as monoclonal antibodies and their toxin conjugates, all metastatic tumors develop resistance, and nearly one-third of HER2+ breast cancer patients develop resistance to all these therapies. Although antibody therapy has shown promising results in breast cancer patients, passive immunotherapy approaches have limitations and need continuous administration over a long period. Vaccine therapy introduces antigens that act on cancer cells causing prolonged activation of the immune system. In particular, cancer relapse could be avoided due to the presence of a longer period of immunological memory with an effective vaccine that can protect against various tumor antigens. Cancer vaccines are broadly classified as preventive and therapeutic. Preventive vaccines are used to ward off any future infections and therapeutic vaccines are used to treat a person with active disease. In this article, we provided details about the tumor environment, different types of vaccines, their advantages and disadvantages, and the current status of various vaccine candidates with a focus on vaccines for breast cancer. Current data indicate that therapeutic vaccines themselves have limitations in terms of efficacy and are used in combination with other chemotherapeutic or targeting agents. The majority of breast cancer vaccines are undergoing clinical trials and the next decade will see the fruitfulness of breast cancer vaccine therapy.
MeSH term(s)	Animals ; Breast Neoplasms/pathology ; Breast Neoplasms/prevention & control ; Cancer Vaccines/therapeutic use ; Female ; Humans ; Neoplasms/pathology ; Neoplasms/prevention & control ; Receptor, ErbB-2/analysis ; Tumor Microenvironment
Chemical Substances	Cancer Vaccines ; ERBB2 protein, human (EC 2.7.10.1) ; Receptor, ErbB-2 (EC 2.7.10.1)
Language	English
Publishing date	2021-01-14
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms22020779
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Article ; Online: Development and evaluation of paclitaxel nanoemulsion for cancer therapy.

Shakhwar, Sara / Darwish, Rana / Kamal, Mohammad M / Nazzal, Sami / Pallerla, Sandeep / Abu Fayyad, Ahmed

Pharmaceutical development and technology

2019 Volume 25, Issue 4, Page(s) 510–516

Abstract: Tocosol™ is a tocopherol-based paclitaxel (PTX) nanoemulsion consisting of α-tocopherol (α-T) isomer of vitamin E as a solubilizer and vitamin E TPGS as the primary emulsifier. Despite its positive attributes in early clinical studies, it failed the ... ...

Abstract	Tocosol™ is a tocopherol-based paclitaxel (PTX) nanoemulsion consisting of α-tocopherol (α-T) isomer of vitamin E as a solubilizer and vitamin E TPGS as the primary emulsifier. Despite its positive attributes in early clinical studies, it failed the pivotal phase III clinical trials. The long-term goal of this work was to reformulate Tocosol™. In this study, Tocosol™ formulation was optimized by replacing the α-T isomer with the more pharmacological active isomer γ-tocotrienol (γ-T
MeSH term(s)	Antineoplastic Agents/administration & dosage ; Antineoplastic Agents/pharmacology ; Cell Line, Tumor ; Chromans/chemistry ; Emulsions/chemistry ; Humans ; Paclitaxel/administration & dosage ; Paclitaxel/pharmacology ; Pancreatic Neoplasms/drug therapy ; Polyethylene Glycols/chemistry ; Surface-Active Agents/chemistry ; Vitamin E/analogs & derivatives ; Vitamin E/chemistry
Chemical Substances	Antineoplastic Agents ; Chromans ; Emulsions ; Surface-Active Agents ; Vitamin E (1406-18-4) ; Polyethylene Glycols (3WJQ0SDW1A) ; plastochromanol 8 (4382-43-8) ; Paclitaxel (P88XT4IS4D)
Language	English
Publishing date	2019-12-26
Publishing country	England
Document type	Journal Article
ZDB-ID	1331774-x
ISSN	1097-9867 ; 1083-7450
ISSN (online)	1097-9867
ISSN	1083-7450
DOI	10.1080/10837450.2019.1706564
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Zs.A 5043: Show issues

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Article ; Online: Design of a doxorubicin-peptidomimetic conjugate that targets HER2-positive cancer cells.

Pallerla, Sandeep / Gauthier, Ted / Sable, Rushikesh / Jois, Seetharama D

European journal of medicinal chemistry

2017 Volume 125, Page(s) 914–924

Abstract: Doxorubicin (DOX) belongs to the anthracycline class of drugs that are used in the treatment of various cancers. It has limited cystostatic effects in therapeutic doses, but higher doses can cause cardiotoxicity. In the current approach, we conjugated a ... ...

Abstract	Doxorubicin (DOX) belongs to the anthracycline class of drugs that are used in the treatment of various cancers. It has limited cystostatic effects in therapeutic doses, but higher doses can cause cardiotoxicity. In the current approach, we conjugated a peptidomimetic (Arg-aminonaphthylpropionic acid-Phe, compound 5) known to bind to HER2 protein to DOX via a glutaric anhydride linker. Antiproliferative assays suggest that the DOX-peptidomimetic conjugate has activity in the lower micromolar range. The conjugate exhibited higher toxicity in HER2-overexpressed cells than in MCF-7 and MCF-10A cells that do not overexpress HER2 protein. Cellular uptake studies using confocal microscope experiments showed that the conjugate binds to HER2-overexpressed cells and DOX is taken up into the cells in 4 h compared to conjugate in MCF-7 cells. Binding studies using surface plasmon resonance indicated that the conjugate binds to the HER2 extracellular domain with high affinity compared to compound 5 or DOX alone. The conjugate was stable in the presence of cells with a half-life of nearly 4 h and 1 h in human serum. DOX is released from the conjugate and internalized into the cells in 4 h, causing cellular toxicity. These results suggest that this conjugate can be used to target DOX to HER2-overexpressing cells and can improve the therapeutic index of DOX for HER2-positive cancer.
MeSH term(s)	Antineoplastic Agents/chemistry ; Antineoplastic Agents/pharmacokinetics ; Antineoplastic Agents/pharmacology ; Binding Sites ; Doxorubicin/chemistry ; Doxorubicin/pharmacokinetics ; Doxorubicin/pharmacology ; Female ; Half-Life ; Humans ; MCF-7 Cells ; Peptidomimetics/chemistry ; Peptidomimetics/pharmacokinetics ; Peptidomimetics/pharmacology ; Protein Binding ; Receptor, ErbB-2/analysis
Chemical Substances	Antineoplastic Agents ; Peptidomimetics ; Doxorubicin (80168379AG) ; ERBB2 protein, human (EC 2.7.10.1) ; Receptor, ErbB-2 (EC 2.7.10.1)
Language	English
Publishing date	2017-01-05
Publishing country	France
Document type	Journal Article
ZDB-ID	188597-2
ISSN	1768-3254 ; 0009-4374 ; 0223-5234
ISSN (online)	1768-3254
ISSN	0009-4374 ; 0223-5234
DOI	10.1016/j.ejmech.2016.10.015
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Zs.B 784: Show issues

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Article ; Online: Current and future targeted therapies for non-small-cell lung cancers with aberrant EGF receptors.

Kanthala, Shanthi / Pallerla, Sandeep / Jois, Seetharama

Future oncology (London, England)

2015 Volume 11, Issue 5, Page(s) 865–878

Abstract: Expression of the EGF receptors (EGFRs) is abnormally high in many types of cancer, including 25% of lung cancers. Successful treatments target mutations in the EGFR tyrosine kinase domain with EGFR tyrosine kinase inhibitors (TKIs). However, almost all ... ...

Abstract	Expression of the EGF receptors (EGFRs) is abnormally high in many types of cancer, including 25% of lung cancers. Successful treatments target mutations in the EGFR tyrosine kinase domain with EGFR tyrosine kinase inhibitors (TKIs). However, almost all patients develop resistance to this treatment, and acquired resistance to first-generation TKI has prompted the clinical development of a second generation of EGFR TKI. Because of the development of resistance to treatment of TKIs, there is a need to collect genomic information about EGFR levels in non-small-cell lung cancer patients. Herein, we focus on current molecular targets that have therapies available as well as other targets for which therapies will be available in the near future.
MeSH term(s)	Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Carcinoma, Non-Small-Cell Lung/diagnosis ; Carcinoma, Non-Small-Cell Lung/drug therapy ; Carcinoma, Non-Small-Cell Lung/genetics ; Carcinoma, Non-Small-Cell Lung/metabolism ; DNA Mutational Analysis ; Humans ; Lung Neoplasms/diagnosis ; Lung Neoplasms/drug therapy ; Lung Neoplasms/genetics ; Lung Neoplasms/metabolism ; Molecular Targeted Therapy ; Mutation ; Protein Kinase Inhibitors/pharmacology ; Protein Kinase Inhibitors/therapeutic use ; Receptor, Epidermal Growth Factor/antagonists & inhibitors ; Receptor, Epidermal Growth Factor/chemistry ; Receptor, Epidermal Growth Factor/genetics ; Receptor, Epidermal Growth Factor/metabolism ; Treatment Outcome
Chemical Substances	Antineoplastic Agents ; Protein Kinase Inhibitors ; Receptor, Epidermal Growth Factor (EC 2.7.10.1)
Language	English
Publishing date	2015
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2184533-5
ISSN	1744-8301 ; 1479-6694
ISSN (online)	1744-8301
ISSN	1479-6694
DOI	10.2217/fon.14.312
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Article ; Online: Proximity ligation assay to study protein-protein interactions of proteins on two different cells.

Sable, Rushikesh / Jambunathan, Nithya / Singh, Sitanshu / Pallerla, Sandeep / Kousoulas, Konstantin G / Jois, Seetharama

BioTechniques

2018 Volume 65, Issue 3, Page(s) 149–157

Abstract: Protein-protein interactions (PPI) by homo-, hetero- or oligo-merization in the cellular environment regulate cellular processes. PPI can be inhibited by antibodies, small molecules or peptides, and this inhibition has therapeutic value. A recently ... ...

Abstract	Protein-protein interactions (PPI) by homo-, hetero- or oligo-merization in the cellular environment regulate cellular processes. PPI can be inhibited by antibodies, small molecules or peptides, and this inhibition has therapeutic value. A recently developed method, the proximity ligation assay (PLA), provides detection of PPI in the cellular environment. However, most applications using this assay are for proteins expressed in the same cell. We employ PLA for the first time to study PPI of cell surface proteins on two different cells. Inhibition of PPI using a peptide inhibitor is also quantified using this assay; PLA is used to detect PPI of CD2 and CD58 between Jurkat cells (T cells) and human fibroblast-like synoviocyte-rheumatoid arthritis cells that are important in the immune response in the autoimmune disease rheumatoid arthritis. This assay provides direct evidence of inhibition of PPI of two proteins on different cell surfaces.
MeSH term(s)	Biotechnology/methods ; CD2 Antigens/analysis ; CD2 Antigens/metabolism ; CD58 Antigens/analysis ; CD58 Antigens/metabolism ; Cells, Cultured ; Flow Cytometry ; Histocompatibility Antigens Class II/analysis ; Histocompatibility Antigens Class II/metabolism ; Humans ; Jurkat Cells ; Membrane Proteins/analysis ; Membrane Proteins/chemistry ; Models, Molecular ; Protein Binding ; Proteins/chemistry ; Synoviocytes
Chemical Substances	CD2 Antigens ; CD58 Antigens ; Histocompatibility Antigens Class II ; Membrane Proteins ; Proteins
Language	English
Publishing date	2018-09-27
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	48453-2
ISSN	1940-9818 ; 0736-6205
ISSN (online)	1940-9818
ISSN	0736-6205
DOI	10.2144/btn-2018-0049
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Zs.A 2435: Show issues

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Article ; Online: Design of cyclic and d-amino acids containing peptidomimetics for inhibition of protein-protein interactions of HER2-HER3.

Pallerla, Sandeep / Naik, Himgauri / Singh, Sitanshu / Gauthier, Ted / Sable, Rushikesh / Jois, Seetharama D

Journal of peptide science : an official publication of the European Peptide Society

2018 Volume 24, Issue 2

Abstract: HER2 receptors are surface proteins belonging to the epidermal growth factor family of receptors. Their numbers are elevated in breast, lung, and ovarian cancers. HER2-positive cancers are aggressive, have higher mortality rate, and have a poor prognosis. ...

Abstract	HER2 receptors are surface proteins belonging to the epidermal growth factor family of receptors. Their numbers are elevated in breast, lung, and ovarian cancers. HER2-positive cancers are aggressive, have higher mortality rate, and have a poor prognosis. We have designed peptidomimetics that bind to HER2 and block the HER2-mediated dimerization of epidermal growth factor family of receptors. Among these, a symmetrical cyclic peptidomimetic (compound 18) exhibited antiproliferative activity in HER2-overexpressing lung cancer cell lines with IC
MeSH term(s)	Amino Acid Sequence ; Amino Acids, Cyclic/chemical synthesis ; Amino Acids, Cyclic/pharmacology ; Antineoplastic Agents/chemical synthesis ; Antineoplastic Agents/pharmacology ; Binding Sites ; Binding, Competitive ; Biomarkers, Tumor/antagonists & inhibitors ; Biomarkers, Tumor/genetics ; Biomarkers, Tumor/metabolism ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Female ; Gene Expression ; Humans ; Inhibitory Concentration 50 ; MCF-7 Cells ; Peptidomimetics/chemical synthesis ; Peptidomimetics/pharmacology ; Protein Binding ; Protein Stability ; Receptor, ErbB-2/antagonists & inhibitors ; Receptor, ErbB-2/genetics ; Receptor, ErbB-2/metabolism ; Receptor, ErbB-3/antagonists & inhibitors ; Receptor, ErbB-3/genetics ; Receptor, ErbB-3/metabolism ; Stereoisomerism ; Structure-Activity Relationship
Chemical Substances	Amino Acids, Cyclic ; Antineoplastic Agents ; Biomarkers, Tumor ; Peptidomimetics ; ERBB2 protein, human (EC 2.7.10.1) ; ERBB3 protein, human (EC 2.7.10.1) ; Receptor, ErbB-2 (EC 2.7.10.1) ; Receptor, ErbB-3 (EC 2.7.10.1)
Language	English
Publishing date	2018-02-12
Publishing country	England
Document type	Journal Article
ZDB-ID	1234416-3
ISSN	1099-1387 ; 1075-2617
ISSN (online)	1099-1387
ISSN	1075-2617
DOI	10.1002/psc.3066
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Article ; Online: A peptidomimetic with a chiral switch is an inhibitor of epidermal growth factor receptor heterodimerization.

Kanthala, Shanthi P / Liu, Yong-Yu / Singh, Sitanshu / Sable, Rushikesh / Pallerla, Sandeep / Jois, Seetharama D

Oncotarget

2017 Volume 8, Issue 43, Page(s) 74244–74262

Abstract: Among different types of EGFR dimers, EGFR-HER2 and HER2-HER3 are well known in different types of cancers. Targeting dimerization of EGFR will have a significant impact on cancer therapies. A symmetric peptidomimetic was designed to inhibit the protein- ... ...

Abstract	Among different types of EGFR dimers, EGFR-HER2 and HER2-HER3 are well known in different types of cancers. Targeting dimerization of EGFR will have a significant impact on cancer therapies. A symmetric peptidomimetic was designed to inhibit the protein-protein interaction of EGFR. The peptidomimetic (Cyclo(1,10)PpR (
Language	English
Publishing date	2017-09-26
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.19013
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Article ; Online: Constrained Cyclic Peptides as Immunomodulatory Inhibitors of the CD2:CD58 Protein-Protein Interaction.

Sable, Rushikesh / Durek, Thomas / Taneja, Veena / Craik, David J / Pallerla, Sandeep / Gauthier, Ted / Jois, Seetharama

ACS chemical biology

2016 Volume 11, Issue 8, Page(s) 2366–2374

Abstract: The interaction between the cell-cell adhesion proteins CD2 and CD58 plays a crucial role in lymphocyte recruitment to inflammatory sites, and inhibitors of this interaction have potential as immunomodulatory drugs in autoimmune diseases. Peptides from ... ...

Abstract	The interaction between the cell-cell adhesion proteins CD2 and CD58 plays a crucial role in lymphocyte recruitment to inflammatory sites, and inhibitors of this interaction have potential as immunomodulatory drugs in autoimmune diseases. Peptides from the CD2 adhesion domain were designed to inhibit CD2:CD58 interactions. To improve the stability of the peptides, β-sheet epitopes from the CD2 region implicated in CD58 recognition were grafted into the cyclic peptide frameworks of sunflower trypsin inhibitor and rhesus theta defensin. The designed multicyclic peptides were evaluated for their ability to modulate cell-cell interactions in three different cell adhesion assays, with one candidate, SFTI-a, showing potent activity in the nanomolar range (IC50: 51 nM). This peptide also suppresses the immune responses in T cells obtained from mice that exhibit the autoimmune disease rheumatoid arthritis. SFTI-a was resistant to thermal denaturation, as judged by circular dichroism spectroscopy and mass spectrometry, and had a half-life of ∼24 h in human serum. Binding of this peptide to CD58 was predicted by molecular docking studies and experimentally confirmed by surface plasmon resonance experiments. Our results suggest that cyclic peptides from natural sources are promising scaffolds for modulating protein-protein interactions that are typically difficult to target with small-molecule compounds.
MeSH term(s)	Adjuvants, Immunologic/pharmacology ; Amino Acid Sequence ; Animals ; CD2 Antigens/metabolism ; CD58 Antigens/metabolism ; Cell Adhesion/drug effects ; Cell Line, Tumor ; Circular Dichroism ; Humans ; Mass Spectrometry ; Mice ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Peptides, Cyclic/chemistry ; Peptides, Cyclic/pharmacology ; Protein Binding ; Surface Plasmon Resonance
Chemical Substances	Adjuvants, Immunologic ; CD2 Antigens ; CD58 Antigens ; Peptides, Cyclic
Language	English
Publishing date	2016-08-19
Publishing country	United States
Document type	Journal Article
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.6b00486
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