681465-85-0Relevant articles and documents
ANTIVIRAL HETEROCYCLIC COMPOUNDS
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Page/Page column 222, (2021/04/10)
The present invention discloses compounds of Formula (I), or pharmaceutically acceptable salts, esters, or prodrugs thereof: which inhibit Human Respiratory Syncytial Virus (HRSV) or Human Metapneumovirus (HMPV) inhibitors. The present invention further relates to pharmaceutical compositions comprising the aforementioned compounds for administration to a subject suffering from HRSV or HMPV infection. The invention also relates to methods of treating an HRSV or HMPV infection in a subject by administering a pharmaceutical composition comprising the compounds of the present invention.
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.
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.