152802-65-8Relevant articles and documents
BENZOTHIA(DI)AZEPINE COMPOUNDS AND THEIR USE AS BILE ACID MODULATORS
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Paragraph 0418-0420, (2021/06/11)
The invention relates to certain 1,5-benzothiazepine and 1,2,5-benzothiadiazepine derivatives as defined herein. These compounds are bile acid modulators having apical sodium-dependent bile acid transporter (ASBT) and/or liver bile acid transport (LBAT) inhibitory activity. The invention also relates to pharmaceutical compositions comprising these compounds and to the use of these compounds in the treatment of cardiovascular diseases, fatty acid metabolism and glucose utilization disorders, gastrointestinal diseases and liver diseases.
BENZOTHIA(DI)AZEPINE COMPOUNDS AND THEIR USE AS BILE ACID MODULATORS
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Paragraph 0906-0908, (2019/12/24)
The invention relates to 1,5-benzothiazepine and 1,2,5-benzothiadiazepine derivatives of formula (I). These compounds are bile acid modulators having apical sodium-dependent bile acid transporter (ASBT) and/or liver bile acid transport (LBAT) inhibitory activity. The invention also relates to pharmaceutical compositions comprising these compounds and to the use of these compounds in the treatment of cardiovascular diseases, fatty acid metabolism and glucose utilization disorders, gastrointestinal diseases and liver diseases.
The first fully planar C5-conformation of homooligopeptides prepared from a chiral α-ethylated α,α-disubstituted amino acid: (S)-butylethylglycine (=(2S)-2-amino-2-ethylhexanoic acid)
Imawaka, Naoto,Tanaka, Masakazu,Suemune, Hiroshi
, p. 2823 - 2835 (2007/10/03)
An optically active α-ethylated α,α-disubstituted amino acid, (S)-butylethylglycine (=(2S)-2-amino-2-ethylhexanoic acid; (S)-Beg; (S)-2), was prepared starting from butyl ethyl ketone (1) by the Strecker method and enzymatic kinetic resolution of the racemic amino acid. Homooligopeptides containing (S)-Beg (up to hexapeptide) were synthesized by conventional solution methods. An ethyl ester was used for the protection at the C-terminus, and a trifluoroacetyl group was used for the N-terminus of the peptides. The structures of tri-and tetrapeptides 5 and 6 in the solid state were solved by X-ray crystallographic analysis, and were shown to have a bent planar C5-conformation (tripeptide) and a fully planar C5-conformation (tetrapeptide) (see Figs. 1 and 2, resp.). The IR and 1H-NMR spectra of hexapeptide 8 revealed that the dominant conformation in CDCl3 solution was also a fully planar C5-conformation. These results show for the first time that the preferred conformation of homopeptides containing a chiral α-ethylated α,α-disubstituted amino acid is a planar C5-conformation.