Journal articles: 'Maytansinol'

1

Bénéchie, Michel, and Françoise Khuong-Huu. "Total Synthesis of (−)-Maytansinol." Journal of Organic Chemistry 61, no. 20 (January 1996): 7133–38. http://dx.doi.org/10.1021/jo960363a.

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BENECHIE, M., and F. KHUONG-HUU. "ChemInform Abstract: Total Synthesis of (-)-Maytansinol." ChemInform 28, no. 5 (August 4, 2010): no. http://dx.doi.org/10.1002/chin.199705299.

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Edwards, A., M. Gladstone, P. Yoon, D. Raben, B. Frederick, and T. T. Su. "Combinatorial effect of maytansinol and radiation in Drosophila and human cancer cells." Disease Models & Mechanisms 4, no. 4 (April 18, 2011): 496–503. http://dx.doi.org/10.1242/dmm.006486.

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Moss, Steven J., Linquan Bai, Sabine Toelzer, Brian J. Carroll, Taifo Mahmud, Tin-Wein Yu, and Heinz G. Floss. "Identification of Asm19 as an Acyltransferase Attaching the Biologically Essential Ester Side Chain of Ansamitocins UsingN-Desmethyl-4,5-desepoxymaytansinol, Not Maytansinol, as Its Substrate." Journal of the American Chemical Society 124, no. 23 (June 2002): 6544–45. http://dx.doi.org/10.1021/ja020214b.

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5

Lopus, Manu, Emin Oroudjev, Leslie Wilson, Sharon Wilhelm, Wayne Widdison, Ravi Chari, and Mary Ann Jordan. "Maytansine and Cellular Metabolites of Antibody-Maytansinoid Conjugates Strongly Suppress Microtubule Dynamics by Binding to Microtubules." Molecular Cancer Therapeutics 9, no. 10 (October 2010): 2689–99. http://dx.doi.org/10.1158/1535-7163.mct-10-0644.

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Kowalczyk, Lidia, Rupert Bartsch, Christian F. Singer, and Alex Farr. "Adverse Events of Trastuzumab Emtansine (T-DM1) in the Treatment of HER2-Positive Breast Cancer Patients." Breast Care 12, no. 6 (2017): 401–8. http://dx.doi.org/10.1159/000480492.

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The human epidermal growth factor receptor 2 (HER2) is commonly associated with poor prognosis and is overexpressed in approximately 15-20% of all breast cancers. The introduction of HER2-targeted therapies led to significant improvement in the prognosis of patients with HER2-positive breast cancer, for both early and advanced disease. These targeted therapies include the antibodies trastzumab and pertuzumab, the tyrosine kinase inhibitor lapatinib, and the antibody-drug conjugate trastuzumab emtansine (T-DM1). T-DM1 combines the anti-tumor activity of trastuzumab with that of DM1, a highly potent derivative of the anti-microtubule agent maytansine, resulting in increased anti-tumor activity. Notably, this agent has been demonstrated to be safe and is associated with low toxicity rates. However, maytansinoid, the cytotoxic component of T-DM1, does have the potential to induce various adverse events, particularly radiation necrosis, when used in combination with stereotactic radiosurgery. In this review, we aimed to summarize the current literature regarding T-DM1 safety and toxicity, with special emphasis on the existing landmark studies.

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Pitakbut, Thanet, Michael Spiteller, and Oliver Kayser. "Genome Mining and Gene Expression Reveal Maytansine Biosynthetic Genes from Endophytic Communities Living inside Gymnosporia heterophylla (Eckl. and Zeyh.) Loes. and the Relationship with the Plant Biosynthetic Gene, Friedelin Synthase." Plants 11, no. 3 (January 25, 2022): 321. http://dx.doi.org/10.3390/plants11030321.

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Even though maytansine was first discovered from Celastraceae plants, it was later proven to be an endophytic bacterial metabolite. However, a pure bacterial culture cannot synthesize maytansine. Therefore, an exclusive interaction between plant and endophytes is required for maytansine production. Unfortunately, our understanding of plant–endophyte interaction is minimal, and critical questions remain. For example: how do endophytes synthesize maytansine inside their plant host, and what is the impact of maytansine production in plant secondary metabolites? Our study aimed to address these questions. We selected Gymnosporia heterophylla as our model and used amino-hydroxybenzoic acid (AHBA) synthase and halogenase genes as biomarkers, as these two genes respond to biosynthesize maytansine. As a result, we found a consortium of seven endophytes involved in maytansine production in G. heterophylla, based on genome mining and gene expression experiments. Subsequently, we evaluated the friedelin synthase (FRS) gene’s expression level in response to biosynthesized 20-hydroxymaytenin in the plant. We found that the FRS expression level was elevated and linked with the expression of the maytansine biosynthetic genes. Thus, we achieved our goals and provided new evidence on endophyte–endophyte and plant–endophyte interactions, focusing on maytansine production and its impact on plant metabolite biosynthesis in G. heterophylla.

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Cao, Shuo, Yue-Hui Dong, De-Feng Wang, and Zhao-Peng Liu. "Tubulin Maytansine Site Binding Ligands and their Applications as MTAs and ADCs for Cancer Therapy." Current Medicinal Chemistry 27, no. 27 (August 5, 2020): 4567–76. http://dx.doi.org/10.2174/0929867327666200316144610.

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Background: Microtubule Targeting Agents (MTAs) represent the most successful anticancer drugs for cancer chemotherapy. Through interfering with the tubulin polymerization and depolymerization dynamics, MTAs influence intracellular transport and cell signal pathways, inhibit cell mitosis and cell proliferation, and induce cell apoptosis and death. The tubulin maytansine site binding agents are natural or nature-derived products that represent one type of the MTAs that inhibit tubulin polymerization and exhibit potent antitumor activity both in vitro and in vivo. They are used as Antibody-Drug Conjugates (ADCs) in cancer chemotherapy. Methods: Using SciFinder® as a tool, the publications about maytansine, its derivatives, maytansine binding site, maytansine site binding agents and their applications as MTAs for cancer therapy were surveyed with an exclusion on those published as patents. The latest progresses in clinical trials were obtained from the clinical trial web. Results: This article presents an introduction about MTAs, maytansine, maytansine binding site and its ligands, the applications of these ligands as MTAs and ADCs in cancer therapy. Conclusion: The maytansine site binding agents are powerful MTAs for cancer chemotherapy. The maytansine site ligands-based ADCs are used in clinic or under clinical trials as cancer targeted therapy to improve their selectivity and to reduce their side effects. Further improvements in the delivery efficiency of the ADCs will benefit the patients in cancer targeted therapy.

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9

Tassone, Pierfrancesco, Victor S. Goldmacher, Paola Neri, Antonella Gozzini, Masood A. Shammas, Kathleen R. Whiteman, Linda L. Hylander-Gans, et al. "Cytotoxic activity of the maytansinoid immunoconjugate B-B4–DM1 against CD138+ multiple myeloma cells." Blood 104, no. 12 (December 1, 2004): 3688–96. http://dx.doi.org/10.1182/blood-2004-03-0963.

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We tested the in vitro and in vivo antitumor activity of the maytansinoid DM1 (N2′-deacetyl-N2′-(3-mercapto-1-oxopropyl)-maytansine), a potent antimicrotubule agent, covalently linked to the murine monoclonal antibody (mAb) B-B4 targeting syndecan-1 (CD138). We evaluated the in vitro activity of B-B4–DM1 against a panel of CD138+ and CD138- cell lines, as well as CD138+ patient multiple myeloma (MM) cells. Treatment with B-B4–DM1 selectively decreased growth and survival of MM cell lines, patient MM cells, and MM cells adherent to bone marrow stromal cells. We further examined the activity of B-B4–DM1 in 3 human MM models in mice: (1) severe combined immunodeficient (SCID) mice bearing subcutaneous xenografts; (2) SCID mice bearing green fluorescent protein–positive (GFP+) xenografts; and (3) SCID mice implanted with human fetal bone (SCID-hu) and subsequently injected with patient MM cells. Tumor regression and inhibition of tumor growth, improvement in overall survival, and reduction in levels of circulating human paraprotein were observed in mice treated with B-B4–DM1. Although immunohistochemical analysis demonstrates restricted CD138 expression in human tissues, the lack of B-B4 reactivity with mouse tissues precludes evaluation of its toxicity in these models. In conclusion, B-B4–DM1 is a potent anti-MM agent that kills cells in an antigen-dependent manner in vitro and mediates in vivo antitumor activity at doses that are well tolerated, providing the rationale for clinical trials of this immunoconjugate in MM.

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10

Tassone, Pierfrancesco, Antonella Gozzini, Victor Goldmacher, Masood A. Shammas, Kathleen R. Whiteman, Daniel R. Carrasco, Cheng Li, et al. "In Vitro and in Vivo Activity of the Maytansinoid Immunoconjugate huN901-N2′-Deacetyl-N2′-(3-Mercapto-1-Oxopropyl)-Maytansine against CD56+ Multiple Myeloma Cells." Cancer Research 64, no. 13 (July 1, 2004): 4629–36. http://dx.doi.org/10.1158/0008-5472.can-04-0142.

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11

Huang, Yuan-Yuan, Lu Chen, Guo-Xu Ma, Xu-Dong Xu, Xue-Gong Jia, Fu-Sheng Deng, Xue-Jian Li, and Jing-Quan Yuan. "A Review on Phytochemicals of the Genus Maytenus and Their Bioactive Studies." Molecules 26, no. 15 (July 28, 2021): 4563. http://dx.doi.org/10.3390/molecules26154563.

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The genus Maytenus is a member of the Celastraceae family, of which several species have long been used in traditional medicine. Between 1976 and 2021, nearly 270 new compounds have been isolated and elucidated from the genus Maytenus. Among these, maytansine and its homologues are extremely rare in nature. Owing to its unique skeleton and remarkable bioactivities, maytansine has attracted many synthetic endeavors in order to construct its core structure. In this paper, the current status of the past 45 years of research on Maytenus, with respect to its chemical and biological activities are discussed. The chemical research includes its structural classification into triterpenoids, sesquiterpenes and alkaloids, along with several chemical synthesis methods of maytansine or maytansine fragments. The biological activity research includes activities, such as anti-tumor, anti-bacterial and anti-inflammatory activities, as well as HIV inhibition, which can provide a theoretical basis for the better development and utilization of the Maytenus.

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12

Erickson, Hans K., and John M. Lambert. "ADME of Antibody–Maytansinoid Conjugates." AAPS Journal 14, no. 4 (August 9, 2012): 799–805. http://dx.doi.org/10.1208/s12248-012-9386-x.

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13

Wang, Hangxiang, Jiaping Wu, Li Xu, Ke Xie, Chao Chen, and Yuehan Dong. "Albumin nanoparticle encapsulation of potent cytotoxic therapeutics shows sustained drug release and alleviates cancer drug toxicity." Chemical Communications 53, no. 17 (2017): 2618–21. http://dx.doi.org/10.1039/c6cc08978j.

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14

Xie, Hai-Na, Yu-Yuan Chen, Guo-Biao Zhu, Hai-Hao Han, Xi-Le Hu, Zhi-Qiang Pan, Yi Zang, et al. "Targeted delivery of maytansine to liver cancer cells via galactose-modified supramolecular two-dimensional glycomaterial." Chemical Communications 58, no. 32 (2022): 5029–32. http://dx.doi.org/10.1039/d1cc06809a.

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15

Suchocki, John A., and Albert T. Sneden. "Characterization of Decomposition Products of Maytansine." Journal of Pharmaceutical Sciences 76, no. 9 (September 1987): 738–43. http://dx.doi.org/10.1002/jps.2600760913.

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16

Helgason, Thorunn, Senthil Damodaran, Kenneth R. Hess, W. Fraser Symmans, and Stacy L. Moulder. "CLO19-036: Folate Receptor alpha Expression in Metastatic Triple-Negative Breast Cancer (TNBC)." Journal of the National Comprehensive Cancer Network 17, no. 3.5 (March 8, 2019): CLO19–036. http://dx.doi.org/10.6004/jnccn.2018.7115.

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Background: Folate receptor alpha (FRα) is a glycosyl phosphatidylinositol (GPI)-anchored cell surface protein that binds and internalizes folate, which is a cofactor required for DNA/RNA synthesis and cell growth and proliferation. There is a marked up-regulation of FRα in many solid tumors; in contrast, FRα has a minimal expression in adult normal tissue. Mirvetuximab soravtansine is an antibody drug conjugate (ADC) consisting of a maytansinoid, N2'-Deacetyl-N2'-(4-mercapto-4-methyl-1-oxopentyl)-maytansine (DM4), conjugated to an anti-FRα antibody, M9346A. Once bound to the FRα and internalized, the anti-mitotic agents are released and inhibit tubulin polymerization and microtubule assembly, leading to cell death. Here we report the expression of FRα+ on residual tumor samples in metastatic TNBC. Methods: 68 patients (Pts) with stage IV TNBC underwent prescreening to determine if residual tumor tissue expressed FRα. Formalin fixed paraffin embedded (FFPE) samples were sent to Ventana Translational Diagnostics CAP/CLIA Laboratory for analysis using an in-house developed assay, Ventana OptiView DAB Detection kit, and the Ventana BenchMark Ultra automated slide stainer. FRα expression was evaluated by board certified pathologists using a scoring scale 1+ (low), 2+ (medium), and 3+ (high). For the purposes of study entry, FRα expression on cell surface was required to be low, defined as >25% of cells having 1+ expression. Results: 12% (8/68) of evaluated TNBCs had moderate to high rates of FRα expression. The median age of pts screened for FRα was 53 years. Moderate to high FRα expression rates were more common in Black and Asian patients (Table 1). Conclusion: Our prospective study has demonstrated that moderate to high expression of FRα in metastatic TNBC is 12%, which is lower than previously reported. An ongoing phase II study will determine efficacy for mirvetuximab soravtansine in advanced TNBC. Acknowledgement: This study was approved and funded in part by the NCCN Oncology Research Program from general research support provided by ImmunoGen, Inc.

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17

Fishkin, Nathan. "Maytansinoid–BODIPY Conjugates: Application to Microscale Determination of Drug Extinction Coefficients and for Quantification of Maytansinoid Analytes." Molecular Pharmaceutics 12, no. 6 (March 16, 2015): 1745–51. http://dx.doi.org/10.1021/mp500843r.

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18

Kusari, Parijat, Souvik Kusari, Dennis Eckelmann, Sebastian Zühlke, Oliver Kayser, and Michael Spiteller. "Cross-species biosynthesis of maytansine in Maytenus serrata." RSC Advances 6, no. 12 (2016): 10011–16. http://dx.doi.org/10.1039/c5ra25042k.

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Cassady, John M., Kenneth K. Chan, Heinz G. Floss, and Eckhard Leistner. "Recent Developments in the Maytansinoid Antitumor Agents." Chemical and Pharmaceutical Bulletin 52, no. 1 (2004): 1–26. http://dx.doi.org/10.1248/cpb.52.1.

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LUDUENA, RICHARD F., WENDY H. ANDERSON, VEENA PRASAD, MARY ANN JORDAN, KATHLEEN C. FERRIGNI, MARY CARMEN ROACH, PAUL M. HOROWITZ, DOUGLAS B. MURPHY, and ARLETTE FELLOUS. "Interactions of Vinblastine and Maytansine with Tubulin." Annals of the New York Academy of Sciences 466, no. 1 Dynamic Aspec (June 1986): 718–32. http://dx.doi.org/10.1111/j.1749-6632.1986.tb38454.x.

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Kusari, Souvik, Marc Lamshöft, Parijat Kusari, Sebastian Gottfried, Sebastian Zühlke, Kathrin Louven, Ute Hentschel, Oliver Kayser, and Michael Spiteller. "Endophytes Are Hidden Producers of Maytansine inPutterlickiaRoots." Journal of Natural Products 77, no. 12 (December 5, 2014): 2577–84. http://dx.doi.org/10.1021/np500219a.

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22

Kovtun, Yelena V., Charlene A. Audette, Michele F. Mayo, Gregory E. Jones, Heather Doherty, Erin K. Maloney, Hans K. Erickson, et al. "Antibody-Maytansinoid Conjugates Designed to Bypass Multidrug Resistance." Cancer Research 70, no. 6 (March 2, 2010): 2528–37. http://dx.doi.org/10.1158/0008-5472.can-09-3546.

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23

Luo, Quanzhou, Hyo Helen Chung, Christopher Borths, Matthew Janson, Jie Wen, Marisa K. Joubert, and Jette Wypych. "Structural Characterization of a Monoclonal Antibody–Maytansinoid Immunoconjugate." Analytical Chemistry 88, no. 1 (December 14, 2015): 695–702. http://dx.doi.org/10.1021/acs.analchem.5b03709.

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Lutz, Robert J., and Kathleen R. Whiteman. "Antibody-maytansinoid conjugates for the treatment of myeloma." mAbs 1, no. 6 (November 2009): 548–51. http://dx.doi.org/10.4161/mabs.1.6.10029.

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Goodwin, Thomas E., Shari G. Orlicek, N. Renee Adams, Lynn A. Covey-Morrison, J. Steve Jenkins, and Gary L. Templeton. "Preparation of an aromatic synthon for maytansinoid synthesis." Journal of Organic Chemistry 50, no. 26 (December 1985): 5889–92. http://dx.doi.org/10.1021/jo00350a098.

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Gao, Shi, Weizhong Zhang, Renjie Wang, Sean P. Hopkins, Jonathan C. Spagnoli, Mohammed Racin, Lin Bai, et al. "Nanoparticles Encapsulating Nitrosylated Maytansine To Enhance Radiation Therapy." ACS Nano 14, no. 2 (January 15, 2020): 1468–81. http://dx.doi.org/10.1021/acsnano.9b05976.

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27

Kirschning, Andreas, Kirsten Harmrolfs, and Tobias Knobloch. "The chemistry and biology of the maytansinoid antitumor agents." Comptes Rendus Chimie 11, no. 11-12 (November 2008): 1523–43. http://dx.doi.org/10.1016/j.crci.2008.02.006.

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Sherman, I. A., R. Boohaker, K. Stinson, P. A. Griffin, and W. A. Hill. "523P AFP-maytansine conjugate: A novel targeted cancer immunotherapy." Annals of Oncology 32 (September 2021): S590—S591. http://dx.doi.org/10.1016/j.annonc.2021.08.1045.

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Widdison, Wayne C., Sharon D. Wilhelm, Emily E. Cavanagh, Kathleen R. Whiteman, Barbara A. Leece, Yelena Kovtun, Victor S. Goldmacher, et al. "Semisynthetic Maytansine Analogues for the Targeted Treatment of Cancer." Journal of Medicinal Chemistry 49, no. 14 (July 2006): 4392–408. http://dx.doi.org/10.1021/jm060319f.

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Takahashi, Masaaki, Shigeo Iwasaki, Hisayoshi Kobayashi, Shigenobu Okuda, Tomoko Murai, and Yoshihiro Sato. "Rhizoxin binding to tubulin at the maytansine-binding site." Biochimica et Biophysica Acta (BBA) - General Subjects 926, no. 3 (December 1987): 215–23. http://dx.doi.org/10.1016/0304-4165(87)90206-6.

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Sherman, Igor A., Rebecca J. Boohaker, Karr Stinson, Patricia Griffin, and Wendy Hill. "An alpha-fetoprotein-maytansine conjugate for the treatment of AFP receptor expressing tumors." Journal of Clinical Oncology 40, no. 16_suppl (June 1, 2022): e15056-e15056. http://dx.doi.org/10.1200/jco.2022.40.16_suppl.e15056.

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e15056 Background: The alpha fetoprotein (AFP) receptor is an oncofetal antigen and a novel target for cancer therapeutics. It is highly expressed on the surfaces of many cancers and myeloid derived suppressor cells (MDSCs) but absent on normal tissues. By conjugating a novel maytansinoid toxin to a recombinant form of human AFP (ACT-101), we can selectively deliver the toxin to cancer and MDSC cells while sparing normal cells, thereby enabling a combination of targeted and immune activating approaches against the tumor. Methods: Four ACT-101-maytansinoid conjugates with different protein-toxin ratios and different linker chemistries were initially investigated in a mouse COLO-205 xenograft model, resulting in the selection of ACT-903 as the lead candidate for further development. A second study performed in the same tumor model compared the effects of single intravenous doses of ACT-903 (10-50 mg/kg) to control groups receiving either vehicle or the unconjugated protein, ACT-101 (25 mg/kg). Tumor growth, survival and clinical observations were assessed for 60 days post tumor implantation. Both serum ACT-101 and maytansinoid levels were measured following the single dose. Results: In the first study, a statistically significant reduction in tumor volume was seen for all four conjugates compared to vehicle control (p < 0.05). For ACT-903, tumors continued shrinking even after treatment completion, becoming undetectable in 9 of 10 animals. All 10 mice in this group survived through Day 60 with no obvious signs of toxicity. In contrast, there were no survivors in the control group. In the single dose study of ACT-903, a significant reduction of tumor burden compared to vehicle was achieved by Day 14 (p < 0.05) in both the 40 and 50 mg/kg dose groups. Mice in these 2 groups received a second dose 15 days after the first dose, based on observed tumor re-growth. Survival was significantly prolonged in the 50 mg/kg (p = 0.0037) and 40 mg/kg group (p < 0.0001) with 7 of 10 in the 50 mg/kg group and 9 of 10 animals in the 40 mg/kg group surviving to Day 60. Similar doses of ACT-101 and ACT-903 produced comparable ACT-101 serum levels, suggesting that the pharmacokinetic profile of the conjugate is driven primarily by the protein component. Free maytansinoid levels at 4 hours were less than 0.01% of the injected dose of the conjugate, indicating that the conjugate is stable in circulation. Conclusions: The efficacy and tolerability of ACT-903 in an animal tumor model supports advancing this conjugate toward clinical use with a regimen of either once a week or once every other week administration.

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Sherman, Igor A., Rebecca J. Boohaker, Karr Stinson, Patricia Griffin, and Wendy Hill. "An alpha-fetoprotein-maytansine conjugate for the treatment of AFP receptor expressing tumors." Journal of Clinical Oncology 40, no. 16_suppl (June 1, 2022): e15056-e15056. http://dx.doi.org/10.1200/jco.2022.40.16_suppl.e15056.

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e15056 Background: The alpha fetoprotein (AFP) receptor is an oncofetal antigen and a novel target for cancer therapeutics. It is highly expressed on the surfaces of many cancers and myeloid derived suppressor cells (MDSCs) but absent on normal tissues. By conjugating a novel maytansinoid toxin to a recombinant form of human AFP (ACT-101), we can selectively deliver the toxin to cancer and MDSC cells while sparing normal cells, thereby enabling a combination of targeted and immune activating approaches against the tumor. Methods: Four ACT-101-maytansinoid conjugates with different protein-toxin ratios and different linker chemistries were initially investigated in a mouse COLO-205 xenograft model, resulting in the selection of ACT-903 as the lead candidate for further development. A second study performed in the same tumor model compared the effects of single intravenous doses of ACT-903 (10-50 mg/kg) to control groups receiving either vehicle or the unconjugated protein, ACT-101 (25 mg/kg). Tumor growth, survival and clinical observations were assessed for 60 days post tumor implantation. Both serum ACT-101 and maytansinoid levels were measured following the single dose. Results: In the first study, a statistically significant reduction in tumor volume was seen for all four conjugates compared to vehicle control (p < 0.05). For ACT-903, tumors continued shrinking even after treatment completion, becoming undetectable in 9 of 10 animals. All 10 mice in this group survived through Day 60 with no obvious signs of toxicity. In contrast, there were no survivors in the control group. In the single dose study of ACT-903, a significant reduction of tumor burden compared to vehicle was achieved by Day 14 (p < 0.05) in both the 40 and 50 mg/kg dose groups. Mice in these 2 groups received a second dose 15 days after the first dose, based on observed tumor re-growth. Survival was significantly prolonged in the 50 mg/kg (p = 0.0037) and 40 mg/kg group (p < 0.0001) with 7 of 10 in the 50 mg/kg group and 9 of 10 animals in the 40 mg/kg group surviving to Day 60. Similar doses of ACT-101 and ACT-903 produced comparable ACT-101 serum levels, suggesting that the pharmacokinetic profile of the conjugate is driven primarily by the protein component. Free maytansinoid levels at 4 hours were less than 0.01% of the injected dose of the conjugate, indicating that the conjugate is stable in circulation. Conclusions: The efficacy and tolerability of ACT-903 in an animal tumor model supports advancing this conjugate toward clinical use with a regimen of either once a week or once every other week administration.

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Catcott, Kalli C., Molly A. McShea, Carl Uli Bialucha, Kathy L. Miller, Stuart W. Hicks, Parmita Saxena, Thomas G. Gesner, et al. "Microscale screening of antibody libraries as maytansinoid antibody-drug conjugates." mAbs 8, no. 3 (January 11, 2016): 513–23. http://dx.doi.org/10.1080/19420862.2015.1134408.

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Goodwin, Thomas E., Kimberley R. Cousins, Heidi M. Crane, Phyllis O. Eason, Timothy E. Freyaldenhoven, Charles C. Harmon, Brock K. King, et al. "Synthesis of Two New Maytansinoid Model Compounds from Carbohydrate Precursors." Journal of Carbohydrate Chemistry 17, no. 3 (April 1998): 323–39. http://dx.doi.org/10.1080/07328309808002895.

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35

Widdison, Wayne, Sharon Wilhelm, Karen Veale, Juliet Costoplus, Gregory Jones, Charlene Audette, Barbara Leece, Laura Bartle, Yelena Kovtun, and Ravi Chari. "Metabolites of Antibody–Maytansinoid Conjugates: Characteristics and in Vitro Potencies." Molecular Pharmaceutics 12, no. 6 (April 8, 2015): 1762–73. http://dx.doi.org/10.1021/mp5007757.

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36

Zhao, Robert Y., Sharon D. Wilhelm, Charlene Audette, Gregory Jones, Barbara A. Leece, Alexandru C. Lazar, Victor S. Goldmacher, et al. "Synthesis and Evaluation of Hydrophilic Linkers for Antibody–Maytansinoid Conjugates." Journal of Medicinal Chemistry 54, no. 10 (May 26, 2011): 3606–23. http://dx.doi.org/10.1021/jm2002958.

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37

Schibler, Matthew J., and Fernando R. Cabral. "Maytansine-resistant mutants of Chinese hamster ovary cells with an alteration in α-tubulin." Canadian Journal of Biochemistry and Cell Biology 63, no. 6 (June 1, 1985): 503–10. http://dx.doi.org/10.1139/o85-069.

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Mutant clones of Chinese hamster ovary cells resistant to killing by the Vinca alkaloid maytansine have been isolated using a single-step procedure. These mutants are threefold more resistant to killing by the drug than the wild-type parent. The majority of the clones (30 of 34) probably contain alterations in membrane permeability based on their cross-resistance to an unrelated drug, puromycin. Two of the four puromycin-sensitive clones were found to contain "extra" spots which migrated close to α-tubulin on two-dimensional gels. The "extra" spots were shown to be electrophoretic variants of α-tubulin with an identical two-dimensional tryptic peptide map to that of the wild-type α-tubulin. The α-tubulin mutants were cross-resistant to other microtubule disrupting drugs such as griseofulvin, vinblastine, and colcemid, but were more sensitive to the microtubule-stabilizing agent taxol than the wild-type parental cells. Mutant – wild-type hybrids were found to be resistant to levels of maytansine intermediate between the lethal doses for mutant and wild-type cells. A possible explanation for the drug resistance of these mutants is discussed.

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Ravry, Mario J. R., George A. Omura, and Robert Birch. "Phase II evaluation of maytansine (NSC 153858) in advanced cancer." American Journal of Clinical Oncology 8, no. 2 (April 1985): 148–50. http://dx.doi.org/10.1097/00000421-198504000-00007.

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39

Kusari, S., P. Kusari, D. Eckelmann, S. Zühlke, O. Kayser, and M. Spiteller. "Novel insights into plant-endophyte communication: maytansine as an example." Planta Medica 81, S 01 (December 14, 2016): S1—S381. http://dx.doi.org/10.1055/s-0036-1596123.

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40

Huang, Abbott B., Chii M. Lin, and Ernest Hamel. "Maytansine inhibits nucleotide binding at the exchangeable site of tubulin." Biochemical and Biophysical Research Communications 128, no. 3 (May 1985): 1239–46. http://dx.doi.org/10.1016/0006-291x(85)91073-3.

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41

Reddy, Joseph A., Elaine Westrick, Hari K. R. Santhapuram, Stephen J. Howard, Michael L. Miller, Marilynn Vetzel, Iontcho Vlahov, Ravi V. J. Chari, Victor S. Goldmacher, and Christopher P. Leamon. "Folate Receptor–Specific Antitumor Activity of EC131, a Folate-Maytansinoid Conjugate." Cancer Research 67, no. 13 (July 1, 2007): 6376–82. http://dx.doi.org/10.1158/0008-5472.can-06-3894.

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42

Oroudjev, Emin, Manu Lopus, Leslie Wilson, Charlene Audette, Carmela Provenzano, Hans Erickson, Yelena Kovtun, Ravi Chari, and Mary Ann Jordan. "Maytansinoid-Antibody Conjugates Induce Mitotic Arrest by Suppressing Microtubule Dynamic Instability." Molecular Cancer Therapeutics 9, no. 10 (October 2010): 2700–2713. http://dx.doi.org/10.1158/1535-7163.mct-10-0645.

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43

Jiang, Zhengyang, Zhen Yang, Feng Li, Zheng Li, Nathan Fishkin, and Kevin Burgess. "Targeted Maytansinoid Conjugate Improves Therapeutic Index for Metastatic Breast Cancer Cells." Bioconjugate Chemistry 29, no. 9 (August 13, 2018): 2920–26. http://dx.doi.org/10.1021/acs.bioconjchem.8b00340.

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44

Ab, O., V. S. Goldmacher, L. M. Bartle, D. Tavares, C. N. Carrigan, S. Xu, M. Okamoto, H. Johnson, K. R. Whiteman, and T. Chittenden. "236 Antibody–maytansinoid conjugates targeting folate receptor 1 for cancer therapy." European Journal of Cancer Supplements 8, no. 7 (November 2010): 77. http://dx.doi.org/10.1016/s1359-6349(10)71941-8.

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45

Lambert, J. M. "Antibody-maytansinoid conjugates: A new strategy for the treatment of cancer." Drugs of the Future 35, no. 6 (2010): 471. http://dx.doi.org/10.1358/dof.2010.035.06.1497487.

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46

Cheng, Hong, Guoqing Xiong, Yi Li, Jiaqi Zhu, Xianghua Xiong, Qingyang Wang, Liancheng Zhang, et al. "Increased yield of AP-3 by inactivation of asm25 in Actinosynnema pretiosum ssp. auranticum ATCC 31565." PLOS ONE 17, no. 3 (March 22, 2022): e0265517. http://dx.doi.org/10.1371/journal.pone.0265517.

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Abstract:

Asamitocins are maytansinoids produced by Actinosynnema pretiosum ssp. auranticum ATCC 31565 (A. pretiosum ATCC 31565), which have a structure similar to that of maytansine, therefore serving as a precursor of maytansine in the development of antibody-drug conjugates (ADCs). Currently, there are more than 20 known derivatives of ansamitocins, among which ansamitocin P-3 (AP-3) exhibits the highest antitumor activity. Despite its importance, the application of AP-3 is restricted by low yield, likely due to a substrate competition mechanism underlying the synthesis pathways of AP-3 and its byproducts. Given that N-demethylansamitocin P-3, the precursor of AP-3, is regulated by asm25 and asm10 to synthesize AGP-3 and AP-3, respectively, asm25 is predicted to be an inhibitory gene for AP-3 production. In this study, we inactivated asm25 in A. pretiosum ATCC 31565 by CRISPR-Cas9-guided gene editing. asm25 depletion resulted in a more than 2-fold increase in AP-3 yield. Surprisingly, the addition of isobutanol further improved AP-3 yield in the asm25 knockout strain by more than 6 times; in contrast, only a 1.53-fold increase was found in the WT strain under the parallel condition. Thus, we uncovered an unknown function of asm25 in AP-3 yield and identified asm25 as a promising target to enhance the large-scale industrial production of AP-3.

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Luduena, Richard F., Mary Carmen Roach, Thomas H. MacRae, and George M. Langford. "N,N′-Ethylene-bis(iodoacetamide) as a probe for structural and functional characteristics of brine shrimp, squid, and bovine tubulins." Canadian Journal of Biochemistry and Cell Biology 63, no. 6 (June 1, 1985): 439–47. http://dx.doi.org/10.1139/o85-063.

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We have developed a simple probe for certain functionally significant features of the tubulin molecule. When bovine brain tubulin is treated with N,N′-ethylene-bis(iodoacetamide) (EBI), two intrachain cross-links, designated βs and β*, are formed in β-tubulin, each one with a unique effect on the electrophoretic mobility of β on gels containing sodium dodecyl sulfate. Formation of the β* cross-link, which involves at least one assembly-critical sulfhydryl, is completely inhibited by colchicine and its congeners, while that of βs is inhibited completely by maytansine and GTP and partly by vinblastine. To see how conserved this complex pattern is in evolution we examined tubulins from the brine shrimp Artemia and the squid Loligo. In both tubulins EBI forms the β* cross-link in a reaction inhibitable by colchicine, podophyllotoxin, and nocodazole. In each tubulin, EBI appears to form a second intrachain cross-link in a reaction that can be inhibited completely by maytansine and GTP and partly by vinblastine. In Artemia, this cross-link alters the electrophoretic mobility to a slightly smaller extent than is the case for βs in bovine brain, but in Loligo the alteration is much greater. It seems that the ligand-binding sites, the critical sulfhydryls, and their spatial interrelationships are strongly conserved and that the βs sulfhydryls or the sequence between them are less strongly conserved in evolution.

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Goldmacher, Victor S., Charlene A. Audette, Yinghua Guan, Eriene-Heidi Sidhom, Jagesh V. Shah, Kathleen R. Whiteman, and Yelena V. Kovtun. "High-Affinity Accumulation of a Maytansinoid in Cells via Weak Tubulin Interaction." PLOS ONE 10, no. 2 (February 11, 2015): e0117523. http://dx.doi.org/10.1371/journal.pone.0117523.

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49

Hodgson, David M., Philip J. Parsons, and Peter A. Stones. "A short and efficient synthesis of a key intermediate for maytansinoid construction." Journal of the Chemical Society, Chemical Communications, no. 3 (1988): 217. http://dx.doi.org/10.1039/c39880000217.

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Sun, Xiuxia, Wayne Widdison, Michele Mayo, Sharon Wilhelm, Barbara Leece, Ravi Chari, Rajeeva Singh, and Hans Erickson. "Design of Antibody−Maytansinoid Conjugates Allows for Efficient Detoxification via Liver Metabolism." Bioconjugate Chemistry 22, no. 4 (April 20, 2011): 728–35. http://dx.doi.org/10.1021/bc100498q.

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Journal articles on the topic 'Maytansinol'

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