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Org Lett

Title:		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
Author(s):		McBrayer DN; Gantman BK; Cameron CD; Tal-Gan Y;
Address:		"Department of Chemistry, University of Nevada, Reno , 1664 North Virginia Street, Reno, Nevada 89557, United States"
Journal Title:		Org Lett
Year:		2017
Volume:		20170607
Issue:		12
Page Number:		3295 - 3298
DOI:		10.1021/acs.orglett.7b01444
ISSN/ISBN:		1523-7052 (Electronic) 1523-7060 (Print) 1523-7052 (Linking)
Abstract:		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
Keywords:		"Bacterial Proteins Enterococcus faecalis Lactones Molecular Structure Peptides, Cyclic Quorum Sensing *Solid-Phase Synthesis Techniques Structure-Activity Relationship;"
Notes:		"MedlineMcBrayer, Dominic N Gantman, Brooke K Cameron, Crissey D Tal-Gan, Yftah eng P20 GM103440/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't 2017/06/08 Org Lett. 2017 Jun 16; 19(12):3295-3298. doi: 10.1021/acs.orglett.7b01444. Epub 2017 Jun 7"