1006030-92-7Relevant academic research and scientific papers
The Albicidin Resistance Factor AlbD Is a Serine Endopeptidase That Hydrolyzes Unusual Oligoaromatic-Type Peptides
Vieweg, Laura,Kretz, Julian,Pesic, Alexander,Kerwat, Dennis,Gr?tz, Stefan,Royer, Monique,Cociancich, Stéphane,Mainz, Andi,Süssmuth, Roderich D.
supporting information, p. 7608 - 7611 (2015/07/02)
The para-aminobenzoic acid-containing peptide albicidin is a pathogenicity factor synthesized by Xanthomonas albilineans in infections of sugar cane. Albicidin is a nanomolar inhibitor of the bacterial DNA gyrase with a strong activity against various Gram-negative bacteria. The bacterium Pantoea dispersa expresses the hydrolase AlbD, conferring natural resistance against albicidin. We show that AlbD is a novel type of endopeptidase that catalyzes the cleavage of albicidin at a peptide backbone amide bond, thus abolishing its antimicrobial activity. Additionally, we determined the minimal cleavage motif of AlbD with substrates derived by chemical synthesis. Our results clearly identify AlbD as a unique endopeptidase that is the first member of a new subfamily of peptidases. Our findings provide the molecular basis for a natural detoxification mechanism, potentially rendering a new tool in biological chemistry approaches.
Design and synthesis of oligoamide-based double α-helix mimetics
Kulikov, Oleg V.,Thompson, Sam,Xu, Hai,Incarvito, Christopher D.,Scott, Richard T.W.,Saraogi, Ishu,Nevola, Laura,Hamilton, Andrew D.
, p. 3433 - 3445 (2013/07/05)
An extensive series of bis-oligobenzamides and bis-oligopyridylamides have been efficiently prepared and studied by X-ray analysis and computational methods. A modular synthesis led to double α-helix mimics bearing between two and ten branched side-chains. The inter-helix angle and distance can be tuned by varying the length and rigidity of the spacer, thereby reproducing the recognition domains of a range of super-secondary structures.
Relaxation of the rigid backbone of an oligoamide-foldamer-based α-helix mimetic: Identification of potent Bcl-xL inhibitors
Yap, Jeremy L.,Cao, Xiaobo,Vanommeslaeghe, Kenno,Jung, Kwan-Young,Peddaboina, Chander,Wilder, Paul T.,Nan, Anjan,MacKerell, Alexander D.,Smythe, W. Roy,Fletcher, Steven
supporting information; experimental part, p. 2928 - 2933 (2012/05/07)
By conducting a structure-activity relationship study of the backbone of a series of oligoamide-foldamer-based α-helix mimetics of the Bak BH3 helix, we have identified especially potent inhibitors of Bcl-xL. The most potent compound has a Ki value of 94 nM in vitro, and single-digit micromolar IC50 values against the proliferation of several Bcl-xL-overexpressing cancer cell lines. The Royal Society of Chemistry 2012.
Synthesis of functionalised aromatic oligamide rods
Plante, Jeffrey,Campbell, Fred,Malkova, Barbora,Kilner, Colin,Warriner, Stuart L.,Wilson, Andrew J.
, p. 138 - 146 (2008/09/20)
A current goal in synthetic chemistry is the design and synthesis of molecules that adopt well defined conformations - so called foldamers. In this manuscript we describe a modular approach for construction of rod shaped para-oligobenzamide molecules. Our approach permits regiospecific incorporation of side chains through a phenolic ether linkage on the scaffold; a feature that partly restricts the conformation of the rod through intramolecular hydrogen-bonding. The Royal Society of Chemistry 2008.
