brevetoxin-b and yessotoxin

brevetoxin-b has been researched along with yessotoxin* in 2 studies

Other Studies

2 other study(ies) available for brevetoxin-b and yessotoxin

Article	Year
Interaction of ladder-shaped polyethers with transmembrane alpha-helix of glycophorin A as evidenced by saturation transfer difference NMR and surface plasmon resonance. Bioorganic & medicinal chemistry letters, 2008, Dec-01, Volume: 18, Issue:23 Ladder-shaped polyether (LSP) compounds are thought to interact with transmembrane alpha-helices, but direct evidence has scarcely obtained for these interactions. We adopted a transmembrane alpha-helix of glycophorin A, and quantitatively evaluated its interaction with LSPs such as yessotoxin (YTX), desulfated YTX and artificial LSPs, using surface plasmon resonance and saturation transfer difference NMR. As a result, dissociation constants (K(D)) of YTX and desulfated YTX to a transmembrane domain peptide of glycophorin A were determined to be in the submillimolar range. Furthermore, in saturation transfer difference NMR, the signals at the polyene side chain and the angular methyl groups of YTX were significantly attenuated, which probably comprised an interacting interface of LSPs with a transmembrane alpha-helix. These results suggest that hydrophobic interaction plays an important role in molecular recognition of the alpha-helix peptide by LSPs. Topics: Ciguatoxins; Ethers; Glycophorins; Magnetic Resonance Spectroscopy; Marine Toxins; Membrane Proteins; Models, Molecular; Molecular Structure; Mollusk Venoms; Oxocins; Polymers; Structure-Activity Relationship	2008
Design and synthesis of an artificial ladder-shaped polyether that interacts with glycophorin A. Bioorganic & medicinal chemistry letters, 2006, Dec-15, Volume: 16, Issue:24 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 alpha-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(alpha)-Hcdots, three dots, centeredO) with the GXXXG motif. Topics: Ciguatoxins; Ethers; Ethers, Cyclic; Glycophorins; Marine Toxins; Models, Molecular; Molecular Conformation; Mollusk Venoms; Oxocins	2006

Article

Year

Interaction of ladder-shaped polyethers with transmembrane alpha-helix of glycophorin A as evidenced by saturation transfer difference NMR and surface plasmon resonance.

Bioorganic & medicinal chemistry letters, 2008, Dec-01, Volume: 18, Issue:23

Ladder-shaped polyether (LSP) compounds are thought to interact with transmembrane alpha-helices, but direct evidence has scarcely obtained for these interactions. We adopted a transmembrane alpha-helix of glycophorin A, and quantitatively evaluated its interaction with LSPs such as yessotoxin (YTX), desulfated YTX and artificial LSPs, using surface plasmon resonance and saturation transfer difference NMR. As a result, dissociation constants (K(D)) of YTX and desulfated YTX to a transmembrane domain peptide of glycophorin A were determined to be in the submillimolar range. Furthermore, in saturation transfer difference NMR, the signals at the polyene side chain and the angular methyl groups of YTX were significantly attenuated, which probably comprised an interacting interface of LSPs with a transmembrane alpha-helix. These results suggest that hydrophobic interaction plays an important role in molecular recognition of the alpha-helix peptide by LSPs.

Topics: Ciguatoxins; Ethers; Glycophorins; Magnetic Resonance Spectroscopy; Marine Toxins; Membrane Proteins; Models, Molecular; Molecular Structure; Mollusk Venoms; Oxocins; Polymers; Structure-Activity Relationship

2008

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

Bioorganic & medicinal chemistry letters, 2006, Dec-15, Volume: 16, Issue:24

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 alpha-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(alpha)-Hcdots, three dots, centeredO) with the GXXXG motif.

Topics: Ciguatoxins; Ethers; Ethers, Cyclic; Glycophorins; Marine Toxins; Models, Molecular; Molecular Conformation; Mollusk Venoms; Oxocins

2006