Design and synthesis of an artificial ladder-shaped polyether that interacts with glycophorin A

Kohei Torikai; Hiroshi Yari; Megumi Mori; Satoru Ujihara; Nobuaki Matsumori; Michio Murata; Tohru Oishi

doi:10.1016/j.bmcl.2006.09.004

Design and synthesis of an artificial ladder-shaped polyether that interacts with glycophorin A

Kohei Torikai, Hiroshi Yari, Megumi Mori, Satoru Ujihara, Nobuaki Matsumori, Michio Murata, Tohru Oishi

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

21 Citations (Scopus)

Abstract

Ladder-shaped polyether (LSP) compounds, such as brevetoxins and ciguatoxins, are thought to interact with transmembrane (TM) proteins. As a model LSP compound, we designed and synthesized an artificial tetracyclic ether (1) and evaluated its interaction with glycophorin A (GpA), a membrane protein known to dimerize or oligomerize between membrane-integral α-helical domains. Model compound 1 was found to induce the dissociation of oligomeric GpA in a similar manner to natural LSPs when examined by SDS-PAGE. The results suggest that even an artificial tetracyclic ether possesses the ability to interact with TM proteins, presumably through the intermolecular hydrogen bonds (C_α-H ⋯ O) with the GXXXG motif.

Original language	English
Pages (from-to)	6355-6359
Number of pages	5
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	16
Issue number	24
DOIs	https://doi.org/10.1016/j.bmcl.2006.09.004
Publication status	Published - Dec 15 2006
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

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10.1016/j.bmcl.2006.09.004

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title = "Design and synthesis of an artificial ladder-shaped polyether that interacts with glycophorin A",

abstract = "Ladder-shaped polyether (LSP) compounds, such as brevetoxins and ciguatoxins, are thought to interact with transmembrane (TM) proteins. As a model LSP compound, we designed and synthesized an artificial tetracyclic ether (1) and evaluated its interaction with glycophorin A (GpA), a membrane protein known to dimerize or oligomerize between membrane-integral α-helical domains. Model compound 1 was found to induce the dissociation of oligomeric GpA in a similar manner to natural LSPs when examined by SDS-PAGE. The results suggest that even an artificial tetracyclic ether possesses the ability to interact with TM proteins, presumably through the intermolecular hydrogen bonds (Cα-H ⋯ O) with the GXXXG motif.",

author = "Kohei Torikai and Hiroshi Yari and Megumi Mori and Satoru Ujihara and Nobuaki Matsumori and Michio Murata and Tohru Oishi",

note = "Funding Information: We are grateful to Dr. Keiichi Konoki in our laboratory for discussion. This work was supported by Grant-in-Aid for Exploratory Research (No. 15655033), for Scientific Research on Priority Areas (No. 16073211) from MEXT.",

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doi = "10.1016/j.bmcl.2006.09.004",

language = "English",

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T1 - Design and synthesis of an artificial ladder-shaped polyether that interacts with glycophorin A

AU - Torikai, Kohei

AU - Yari, Hiroshi

AU - Mori, Megumi

AU - Ujihara, Satoru

AU - Matsumori, Nobuaki

AU - Murata, Michio

AU - Oishi, Tohru

N1 - Funding Information: We are grateful to Dr. Keiichi Konoki in our laboratory for discussion. This work was supported by Grant-in-Aid for Exploratory Research (No. 15655033), for Scientific Research on Priority Areas (No. 16073211) from MEXT.

PY - 2006/12/15

Y1 - 2006/12/15

N2 - Ladder-shaped polyether (LSP) compounds, such as brevetoxins and ciguatoxins, are thought to interact with transmembrane (TM) proteins. As a model LSP compound, we designed and synthesized an artificial tetracyclic ether (1) and evaluated its interaction with glycophorin A (GpA), a membrane protein known to dimerize or oligomerize between membrane-integral α-helical domains. Model compound 1 was found to induce the dissociation of oligomeric GpA in a similar manner to natural LSPs when examined by SDS-PAGE. The results suggest that even an artificial tetracyclic ether possesses the ability to interact with TM proteins, presumably through the intermolecular hydrogen bonds (Cα-H ⋯ O) with the GXXXG motif.

AB - Ladder-shaped polyether (LSP) compounds, such as brevetoxins and ciguatoxins, are thought to interact with transmembrane (TM) proteins. As a model LSP compound, we designed and synthesized an artificial tetracyclic ether (1) and evaluated its interaction with glycophorin A (GpA), a membrane protein known to dimerize or oligomerize between membrane-integral α-helical domains. Model compound 1 was found to induce the dissociation of oligomeric GpA in a similar manner to natural LSPs when examined by SDS-PAGE. The results suggest that even an artificial tetracyclic ether possesses the ability to interact with TM proteins, presumably through the intermolecular hydrogen bonds (Cα-H ⋯ O) with the GXXXG motif.

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IS - 24

ER -

Design and synthesis of an artificial ladder-shaped polyether that interacts with glycophorin A

Abstract

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