Development of BCR-ABL degradation inducers via the conjugation of an imatinib derivative and a cIAP1 ligand
[Display omitted] The manipulation of protein stability with small molecules has great potential as a technique for aiding the development of clinical therapies, including treatments for cancer. In this study, BCR-ABL protein degradation inducers called SNIPER(ABL) (Specific and Non-genetic inhibito...
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| Published in | Bioorganic & medicinal chemistry letters Vol. 26; no. 20; pp. 4865 - 4869 |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
OXFORD
Elsevier Ltd
15.10.2016
Elsevier |
| Subjects | |
| Online Access | Get full text |
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| Abstract | [Display omitted]
The manipulation of protein stability with small molecules has great potential as a technique for aiding the development of clinical therapies, including treatments for cancer. In this study, BCR-ABL protein degradation inducers called SNIPER(ABL) (Specific and Non-genetic inhibitors of apoptosis protein [IAP]-dependent Protein Erasers) were developed. The designed molecules contained two biologically active scaffolds: one was an imatinib derivative that binds to BCL-ABL and the other was a methyl bestatin that binds to cellular IAP 1 (cIAP1). The hybrid molecules, SNIPER(ABL), were expected to recruit BCR-ABL to cIAP1 for removal by proteasomes. In fact, SNIPER(ABL) induced the degradation of BCR-ABL protein and a subsequent reduction in cell growth. Thus, the degradation of BCR-ABL by SNIPER(ABL) is one potential strategy for treating BCR-ABL driven chronic myelogenous leukemia. |
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| AbstractList | [Display omitted]
The manipulation of protein stability with small molecules has great potential as a technique for aiding the development of clinical therapies, including treatments for cancer. In this study, BCR-ABL protein degradation inducers called SNIPER(ABL) (Specific and Non-genetic inhibitors of apoptosis protein [IAP]-dependent Protein Erasers) were developed. The designed molecules contained two biologically active scaffolds: one was an imatinib derivative that binds to BCL-ABL and the other was a methyl bestatin that binds to cellular IAP 1 (cIAP1). The hybrid molecules, SNIPER(ABL), were expected to recruit BCR-ABL to cIAP1 for removal by proteasomes. In fact, SNIPER(ABL) induced the degradation of BCR-ABL protein and a subsequent reduction in cell growth. Thus, the degradation of BCR-ABL by SNIPER(ABL) is one potential strategy for treating BCR-ABL driven chronic myelogenous leukemia. The manipulation of protein stability with small molecules has great potential as a technique for aiding the development of clinical therapies, including treatments for cancer. In this study, BCR-ABL protein degradation inducers called SNIPER(ABL) (Specific and Non-genetic inhibitors of apoptosis protein [IAP]-dependent Protein Erasers) were developed. The designed molecules contained two biologically active scaffolds: one was an imatinib derivative that binds to BCL-ABL and the other was a methyl bestatin that binds to cellular IAP 1 (cIAP1). The hybrid molecules, SNIPER(ABL), were expected to recruit BCR-ABL to cIAP1 for removal by proteasomes. In fact, SNIPER(ABL) induced the degradation of BCR-ABL protein and a subsequent reduction in cell growth. Thus, the degradation of BCR-ABL by SNIPER(ABL) is one potential strategy for treating BCR-ABL driven chronic myelogenous leukemia. The manipulation of protein stability with small molecules has great potential as a technique for aiding the development of clinical therapies, including treatments for cancer. In this study, BCR-ABL protein degradation inducers called SNIPER(ABL) (Specific and Non-genetic inhibitors of apoptosis protein [IAP]-dependent Protein Erasers) were developed. The designed molecules contained two biologically active scaffolds: one was an imatinib derivative that binds to BCL-ABL and the other was a methyl bestatin that binds to cellular IAP 1 (cIAP1). The hybrid molecules, SNIPER(ABL), were expected to recruit BCR-ABL to cIAP1 for removal by proteasomes. In fact, SNIPER(ABL) induced the degradation of BCR-ABL protein and a subsequent reduction in cell growth. Thus, the degradation of BCR-ABL by SNIPER(ABL) is one potential strategy for treating BCR-ABL driven chronic myelogenous leukemia.The manipulation of protein stability with small molecules has great potential as a technique for aiding the development of clinical therapies, including treatments for cancer. In this study, BCR-ABL protein degradation inducers called SNIPER(ABL) (Specific and Non-genetic inhibitors of apoptosis protein [IAP]-dependent Protein Erasers) were developed. The designed molecules contained two biologically active scaffolds: one was an imatinib derivative that binds to BCL-ABL and the other was a methyl bestatin that binds to cellular IAP 1 (cIAP1). The hybrid molecules, SNIPER(ABL), were expected to recruit BCR-ABL to cIAP1 for removal by proteasomes. In fact, SNIPER(ABL) induced the degradation of BCR-ABL protein and a subsequent reduction in cell growth. Thus, the degradation of BCR-ABL by SNIPER(ABL) is one potential strategy for treating BCR-ABL driven chronic myelogenous leukemia. The manipulation of protein stability with small molecules has great potential as a technique for aiding the development of clinical therapies, including treatments for cancer. In this study, BCR-ABL protein degradation inducers called SNIPER(ABL) (Specific and Non-genetic inhibitors of apoptosis protein [IAP]-dependent Protein Erasers) were developed. The designed molecules contained two biologically active scaffolds: one was an imatinib derivative that binds to BCL-ABL and the other was a methyl bestatin that binds to cellular IAP 1 (cIAP1). The hybrid molecules, SNIPER(ABL), were expected to recruit BCR-ABL to cIAP1 for removal by proteasomes. In fact, SNIPER(ABL) induced the degradation of BCR-ABL protein and a subsequent reduction in cell growth. Thus, the degradation of BCR-ABL by SNIPER (ABL) is one potential strategy for treating BCR-ABL driven chronic myelogenous leukemia. (C) 2016 Elsevier Ltd. All rights reserved. |
| Author | Demizu, Yosuke Kurihara, Masaaki Motoi, Hiromi Misawa, Takashi Shoda, Takuji Naito, Mikihiko Shibata, Norihito Hattori, Takayuki Ohoka, Nobumichi |
| Author_xml | – sequence: 1 givenname: Yosuke orcidid: 0000-0001-7521-4861 surname: Demizu fullname: Demizu, Yosuke email: demizu@nihs.go.jp organization: Division of Organic Chemistry, National Institute of Health Sciences, Tokyo, Japan – sequence: 2 givenname: Norihito surname: Shibata fullname: Shibata, Norihito organization: Division of Molecular Target and Gene Therapy Products, National Institute of Health Sciences, Tokyo, Japan – sequence: 3 givenname: Takayuki surname: Hattori fullname: Hattori, Takayuki organization: Division of Molecular Target and Gene Therapy Products, National Institute of Health Sciences, Tokyo, Japan – sequence: 4 givenname: Nobumichi surname: Ohoka fullname: Ohoka, Nobumichi organization: Division of Molecular Target and Gene Therapy Products, National Institute of Health Sciences, Tokyo, Japan – sequence: 5 givenname: Hiromi surname: Motoi fullname: Motoi, Hiromi organization: Division of Organic Chemistry, National Institute of Health Sciences, Tokyo, Japan – sequence: 6 givenname: Takashi surname: Misawa fullname: Misawa, Takashi organization: Division of Organic Chemistry, National Institute of Health Sciences, Tokyo, Japan – sequence: 7 givenname: Takuji surname: Shoda fullname: Shoda, Takuji organization: Division of Organic Chemistry, National Institute of Health Sciences, Tokyo, Japan – sequence: 8 givenname: Mikihiko surname: Naito fullname: Naito, Mikihiko email: miki-naito@nihs.go.jp organization: Division of Molecular Target and Gene Therapy Products, National Institute of Health Sciences, Tokyo, Japan – sequence: 9 givenname: Masaaki surname: Kurihara fullname: Kurihara, Masaaki email: masaaki@nihs.go.jp organization: Division of Organic Chemistry, National Institute of Health Sciences, Tokyo, Japan |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27666635$$D View this record in MEDLINE/PubMed |
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| Keywords | Protein knockdown Imatinib E3 ubiquitin ligase Bestatin BCR-ABL DESIGN HYBRID MOLECULES TYROSINE KINASE ALPHA CHRONIC MYELOID-LEUKEMIA CELL-DEATH SMALL-MOLECULE PROTACS UBIQUITINATION PHILADELPHIA-CHROMOSOME |
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The manipulation of protein stability with small molecules has great potential as a technique for aiding the development of clinical... The manipulation of protein stability with small molecules has great potential as a technique for aiding the development of clinical therapies, including... |
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| SubjectTerms | BCR-ABL Bestatin Chemistry Chemistry, Medicinal Chemistry, Organic E3 ubiquitin ligase Fusion Proteins, bcr-abl - metabolism Humans Imatinib Imatinib Mesylate - metabolism Inhibitor of Apoptosis Proteins - metabolism K562 Cells Life Sciences & Biomedicine Ligands Pharmacology & Pharmacy Physical Sciences Protein Binding Protein knockdown Proteolysis Science & Technology |
| Title | Development of BCR-ABL degradation inducers via the conjugation of an imatinib derivative and a cIAP1 ligand |
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