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Open AccessCommunication
Mar. Drugs 2015, 13(5), 3061-3071; doi:10.3390/md13053061

SAR of Sponge-Inspired Hemibastadin Congeners Inhibiting Blue Mussel PhenolOxidase

1
Institute of Pharmaceutical Biology and Biotechnology, Heinrich-Heine-University Düsseldorf, Universitätsstrasse 1, Geb. 26.23, 40225 Düsseldorf, Germany
2
LEMAR UMR 6539 UBO CNRS Ifremer IRD, European Institute of Marine Studies (IUEM), Université de Bretagne Occidentale (UBO), European University of Brittany (UEB), Technopole Brest-Iroise, 29280 Plouzané, France
3
Biodimar, Université de Bretagne Occidentale (UBO), European University of Brittany (UEB), 6 Avenue Victor Le Gorgeu, CS93837, 29238 Brest cedex 3, France
*
Author to whom correspondence should be addressed.
Academic Editor: Orazio Taglialatela-Scafati
Received: 27 January 2015 / Revised: 19 April 2015 / Accepted: 5 May 2015 / Published: 15 May 2015
View Full-Text   |   Download PDF [337 KB, uploaded 15 May 2015]   |  

Abstract

Hemibastadin derivatives, including the synthetically-derived 5,5′-dibromohemibastadin-1 (DBHB), are potent inhibitors of blue mussel phenoloxidase (PO), which is a key enzyme involved in the firm attachment of this invertebrate to substrates and, thus, a promising molecular target for anti-fouling research. For a systematic investigation of the enzyme inhibitory activity of hemibastadin derivatives, we have synthesized nine new congeners, which feature structural variations of the DBHB core structure. These structural modifications include, e.g., different halogen substituents present at the aromatic rings, different amine moieties linked to the (E)-2-(hydroxyimino)-3-(4-hydroxyphenyl)propionic acid, the presence of free vs. substituted aromatic hydroxyl groups and a free vs. methylated oxime group. All compounds were tested for their inhibitory activity towards the target enzyme in vitro, and IC50 values were calculated. Derivatives, which structurally closely resemble sponge-derived hemibastadins, revealed superior enzyme inhibitory properties vs. congeners featuring structural moieties that are absent in the respective natural products. This study suggests that natural selection has yielded structurally-optimized antifouling compounds. View Full-Text
Keywords: antifouling; hemibastadin; phenoloxidase; sponges; copper; Mytilus edulis antifouling; hemibastadin; phenoloxidase; sponges; copper; Mytilus edulis
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Niemann, H.; Hagenow, J.; Chung, M.-Y.; Hellio, C.; Weber, H.; Proksch, P. SAR of Sponge-Inspired Hemibastadin Congeners Inhibiting Blue Mussel PhenolOxidase. Mar. Drugs 2015, 13, 3061-3071.

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