Demonstration of direct binding of cIAP1 degradation-promoting bestatin analogs to BIR3 domain: Synthesis and application of fluorescent bestatin ester analogs

Shinichi Sato; Hiroshi Aoyama; Hiroyuki Miyachi; Mikihiko Naito; Yuichi Hashimoto

doi:10.1016/j.bmcl.2008.04.031

Demonstration of direct binding of cIAP1 degradation-promoting bestatin analogs to BIR3 domain: Synthesis and application of fluorescent bestatin ester analogs

Shinichi Sato, Hiroshi Aoyama, Hiroyuki Miyachi, Mikihiko Naito, Yuichi Hashimoto

FRIS - Core Interdisciplinary Research Section

The University of Tokyo

Research output: Contribution to journal › Article › peer-review

32 Citations (Scopus)

Abstract

Overexpression of cIAP1 correlates with resistance to radiotherapy and chemotherapy in various cancers. Recently, we reported that a class of bestatin ester analogs represented by MeBS (2) destabilized and promoted the degradation of cIAP1 through auto-ubiquitination, and thereby sensitized cancer cells to apoptosis. Herein, we present chemical evidence that bestatin ester analogs directly interact with the cIAP1-BIR3 domain by means of fluorescence polarization assay and photoaffinity labeling assay using fluorescent probes.

Original language	English
Pages (from-to)	3354-3358
Number of pages	5
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	18
Issue number	11
DOIs	https://doi.org/10.1016/j.bmcl.2008.04.031
Publication status	Published - 2008 Jun 1

Keywords

Bestatin
BIR3 domain
cIAP1
Fluorescence polarization
Photoaffinity labeling

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.bmcl.2008.04.031

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title = "Demonstration of direct binding of cIAP1 degradation-promoting bestatin analogs to BIR3 domain: Synthesis and application of fluorescent bestatin ester analogs",

abstract = "Overexpression of cIAP1 correlates with resistance to radiotherapy and chemotherapy in various cancers. Recently, we reported that a class of bestatin ester analogs represented by MeBS (2) destabilized and promoted the degradation of cIAP1 through auto-ubiquitination, and thereby sensitized cancer cells to apoptosis. Herein, we present chemical evidence that bestatin ester analogs directly interact with the cIAP1-BIR3 domain by means of fluorescence polarization assay and photoaffinity labeling assay using fluorescent probes.",

keywords = "Bestatin, BIR3 domain, cIAP1, Fluorescence polarization, Photoaffinity labeling",

author = "Shinichi Sato and Hiroshi Aoyama and Hiroyuki Miyachi and Mikihiko Naito and Yuichi Hashimoto",

note = "Funding Information: We are grateful to Nippon Kayaku Co. for providing MeBS. The work described in this letter was partially supported by Grants-in-Aid for Scientific Research from The Ministry of Education, Culture, Sports, Science and Technology, Japan, and the Japan Society for the Promotion of Science.",

year = "2008",

month = jun,

day = "1",

doi = "10.1016/j.bmcl.2008.04.031",

language = "English",

volume = "18",

pages = "3354--3358",

journal = "Bioorganic and Medicinal Chemistry Letters",

issn = "0960-894X",

publisher = "Elsevier Ltd.",

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}

Demonstration of direct binding of cIAP1 degradation-promoting bestatin analogs to BIR3 domain: Synthesis and application of fluorescent bestatin ester analogs. / Sato, Shinichi; Aoyama, Hiroshi; Miyachi, Hiroyuki et al.
In: Bioorganic and Medicinal Chemistry Letters, Vol. 18, No. 11, 01.06.2008, p. 3354-3358.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Demonstration of direct binding of cIAP1 degradation-promoting bestatin analogs to BIR3 domain

T2 - Synthesis and application of fluorescent bestatin ester analogs

AU - Sato, Shinichi

AU - Aoyama, Hiroshi

AU - Miyachi, Hiroyuki

AU - Naito, Mikihiko

AU - Hashimoto, Yuichi

N1 - Funding Information: We are grateful to Nippon Kayaku Co. for providing MeBS. The work described in this letter was partially supported by Grants-in-Aid for Scientific Research from The Ministry of Education, Culture, Sports, Science and Technology, Japan, and the Japan Society for the Promotion of Science.

PY - 2008/6/1

Y1 - 2008/6/1

N2 - Overexpression of cIAP1 correlates with resistance to radiotherapy and chemotherapy in various cancers. Recently, we reported that a class of bestatin ester analogs represented by MeBS (2) destabilized and promoted the degradation of cIAP1 through auto-ubiquitination, and thereby sensitized cancer cells to apoptosis. Herein, we present chemical evidence that bestatin ester analogs directly interact with the cIAP1-BIR3 domain by means of fluorescence polarization assay and photoaffinity labeling assay using fluorescent probes.

AB - Overexpression of cIAP1 correlates with resistance to radiotherapy and chemotherapy in various cancers. Recently, we reported that a class of bestatin ester analogs represented by MeBS (2) destabilized and promoted the degradation of cIAP1 through auto-ubiquitination, and thereby sensitized cancer cells to apoptosis. Herein, we present chemical evidence that bestatin ester analogs directly interact with the cIAP1-BIR3 domain by means of fluorescence polarization assay and photoaffinity labeling assay using fluorescent probes.

KW - Bestatin

KW - BIR3 domain

KW - cIAP1

KW - Fluorescence polarization

KW - Photoaffinity labeling

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U2 - 10.1016/j.bmcl.2008.04.031

DO - 10.1016/j.bmcl.2008.04.031

M3 - Article

C2 - 18448338

AN - SCOPUS:44149100029

SN - 0960-894X

VL - 18

SP - 3354

EP - 3358

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 11

ER -

Demonstration of direct binding of cIAP1 degradation-promoting bestatin analogs to BIR3 domain: Synthesis and application of fluorescent bestatin ester analogs

Abstract

Keywords

UN SDGs

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