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.
| Original language | English |
|---|---|
| Pages (from-to) | 6355-6359 |
| Number of pages | 5 |
| Journal | Bioorganic and Medicinal Chemistry Letters |
| Volume | 16 |
| Issue number | 24 |
| DOIs | |
| Publication status | Published - Dec 15 2006 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Pharmaceutical Science
- Drug Discovery
- Clinical Biochemistry
- Organic Chemistry
Cite this
Design and synthesis of an artificial ladder-shaped polyether that interacts with glycophorin A. / Torikai, Kohei; Yari, Hiroshi; Mori, Megumi; Ujihara, Satoru; Matsumori, Nobuaki; Murata, Michio; Oishi, Tohru.
In: Bioorganic and Medicinal Chemistry Letters, Vol. 16, No. 24, 15.12.2006, p. 6355-6359.Research output: Contribution to journal › Article
}
TY - JOUR
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
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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UR - http://www.scopus.com/inward/citedby.url?scp=33750738565&partnerID=8YFLogxK
U2 - 10.1016/j.bmcl.2006.09.004
DO - 10.1016/j.bmcl.2006.09.004
M3 - Article
C2 - 16989999
AN - SCOPUS:33750738565
VL - 16
SP - 6355
EP - 6359
JO - Bioorganic and Medicinal Chemistry Letters
JF - Bioorganic and Medicinal Chemistry Letters
SN - 0960-894X
IS - 24
ER -