Antifouling bastadin congeners target blue mussel phenoloxidase and complex copper(II) ions

M. Bayer; Claire Hellio; J-P. Marechal; W. Lin; W. Frank; H. Weber; P. Proksch

doi:10.1007/s10126-011-9378-3

Antifouling bastadin congeners target blue mussel phenoloxidase and complex copper(II) ions

M. Bayer, Claire Hellio, J-P. Marechal, W. Lin, W. Frank, H. Weber, P. Proksch

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Abstract

Synthetically prepared congeners of sponge-derived bastadin derivatives such as 5,5′-dibromohemibastadin-1 (DBHB) that suppress the settling of barnacle larvae were identified in this study as strong inhibitors of blue mussel phenoloxidase that is involved in the firm attachment of mussels to a given substrate. The IC50 value of DBHB as the most active enzyme inhibitor encountered in this study amounts to 0.84 μM. Inhibition of phenoloxidase by DBHB is likely due to complexation of copper(II) ions from the catalytic centre of the enzyme by the α-oxo-oxime moiety of the compound as shown here for the first time by structure activity studies and by X-ray structure determination of a copper(II) complex of DBHB.

Original language	English
Pages (from-to)	1148-1158
Number of pages	11
Journal	Marine Biotechnology
Volume	13
Issue number	6
DOIs	https://doi.org/10.1007/s10126-011-9378-3
Publication status	Published - Dec 2011

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title = "Antifouling bastadin congeners target blue mussel phenoloxidase and complex copper(II) ions",

abstract = "Synthetically prepared congeners of sponge-derived bastadin derivatives such as 5,5′-dibromohemibastadin-1 (DBHB) that suppress the settling of barnacle larvae were identified in this study as strong inhibitors of blue mussel phenoloxidase that is involved in the firm attachment of mussels to a given substrate. The IC50 value of DBHB as the most active enzyme inhibitor encountered in this study amounts to 0.84 μM. Inhibition of phenoloxidase by DBHB is likely due to complexation of copper(II) ions from the catalytic centre of the enzyme by the α-oxo-oxime moiety of the compound as shown here for the first time by structure activity studies and by X-ray structure determination of a copper(II) complex of DBHB.",

author = "M. Bayer and Claire Hellio and J-P. Marechal and W. Lin and W. Frank and H. Weber and P. Proksch",

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TY - JOUR

T1 - Antifouling bastadin congeners target blue mussel phenoloxidase and complex copper(II) ions

AU - Bayer, M.

AU - Hellio, Claire

AU - Marechal, J-P.

AU - Lin, W.

AU - Frank, W.

AU - Weber, H.

AU - Proksch, P.

PY - 2011/12

Y1 - 2011/12

N2 - Synthetically prepared congeners of sponge-derived bastadin derivatives such as 5,5′-dibromohemibastadin-1 (DBHB) that suppress the settling of barnacle larvae were identified in this study as strong inhibitors of blue mussel phenoloxidase that is involved in the firm attachment of mussels to a given substrate. The IC50 value of DBHB as the most active enzyme inhibitor encountered in this study amounts to 0.84 μM. Inhibition of phenoloxidase by DBHB is likely due to complexation of copper(II) ions from the catalytic centre of the enzyme by the α-oxo-oxime moiety of the compound as shown here for the first time by structure activity studies and by X-ray structure determination of a copper(II) complex of DBHB.

AB - Synthetically prepared congeners of sponge-derived bastadin derivatives such as 5,5′-dibromohemibastadin-1 (DBHB) that suppress the settling of barnacle larvae were identified in this study as strong inhibitors of blue mussel phenoloxidase that is involved in the firm attachment of mussels to a given substrate. The IC50 value of DBHB as the most active enzyme inhibitor encountered in this study amounts to 0.84 μM. Inhibition of phenoloxidase by DBHB is likely due to complexation of copper(II) ions from the catalytic centre of the enzyme by the α-oxo-oxime moiety of the compound as shown here for the first time by structure activity studies and by X-ray structure determination of a copper(II) complex of DBHB.

U2 - 10.1007/s10126-011-9378-3

DO - 10.1007/s10126-011-9378-3

M3 - Article

SN - 1436-2228

VL - 13

SP - 1148

EP - 1158

JO - Marine Biotechnology

JF - Marine Biotechnology

IS - 6

ER -

Antifouling bastadin congeners target blue mussel phenoloxidase and complex copper(II) ions

Abstract

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