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The development of an entirely solid-phase peptide synthesis (SPPS)-based synthesis of the quorum sensing signal gelatinase biosynthesis-activating pheromone (GBAP) from Enterococcus faecalis is reported. The method was used to prepare three libraries of analogues to investigate the structure-activity relationships (SARs) of the GBAP signal. The SAR studies revealed new characteristics of the GBAP signal and uncovered the most potent quorum sensing activator in E. faecalis known to date.

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An Entirely Solid Phase Peptide Synthesis-Based Strategy for Synthesis of Gelatinase Biosynthesis-Activating Pheromone (GBAP) Analogue Libraries: Investigating the Structure–Activity Relationships of the <i>Enterococcus faecalis</i> Quorum Sensing Signal

An Entirely Solid Phase Peptide Synthesis-Based Strategy for Synthesis of Gelatinase Biosynthesis-Activating Pheromone (GBAP) Analogue Libraries: Investigating the Structure–Activity Relationships of the Enterococcus faecalis Quorum Sensing Signal