684643-49-0Relevant academic research and scientific papers
Exploring β-hydroxy γ-amino acids (statines) in the design of hybrid peptide foldamers
Bandyopadhyay, Anupam,Malik, Ankita,Kumar, Mothukuri Ganesh,Gopi, Hosahudya N.
, p. 294 - 297 (2014)
The synthesis and characterization of syn and anti β-hydroxy γ-amino acid (statine) diastereoisomers, their utilization in the design of hybrid peptide foldamers, and their single crystal conformations are studied.
Synthesis and docking studies of renin inhibitors containing ester and amide derivatives of (3S, 4S)-4-amino-hydroxy acids with S3-S3’ renin binding site
Winiecka, Iwona,Marsza?ek, Dorota,Jaworski, Pawe?,Mazurek, Andrzej,P?cak, Paulina,Winiecki, Kajetan,Wierzbowski, Artur
, p. 55 - 70 (2021/05/07)
Seven novel potential renin inhibitors, having a structure based on the peptide fragment 8-13 of human angiotensinogen - a natural substrate for renin, have been designed and synthesized. All peptides were obtained by the carbodiimide method in solution and purified by chromatography on the SiO2 column. In P1-P3’ positions, they contain esters or N-alkyl amides of modified (3S, 4S)-4-amino-3-hydroxyacids. The achieved inhibitory activity IC50 was of 10-6-10-7M Inhibitory activity of the compounds was measured in vitro by high-performance liquid chromatography (HPLC) determination of lowering the concentration of substrate in the presence of renin and the potential rennin inhibitor. Their resistance to enzymatic degradation was assayed by the determination of stability against chymotrypsin activity. Their hydrophobicity evaluated as a Log P-value was calculated by a computer method. The theoretical binding affinity of thus obtained inhibitors was elaborated based on docking to the S3-S3’ pocket of the renin active site.
Stereoselective synthesis of four possible isomers of streptopyrrolidine
Mohapatra, Debendra K.,Thirupathi, Barla,Das, Pragna P.,Yadav, Jhillu S.
experimental part, p. 34 - 39 (2011/03/22)
The synthesis of (4R,5R)-streptopyrrolidine (1), (4S,5R)-streptopyrrolidine (2) (4R, 5S)-streptopyrrolidine (3) and (4S,5S)-strepto- pyrrolidine (4) have been achieved in a concise and highly efficient manner via a highly stereoselective aldol type reacti
New potential renin inhibitors with dipeptide replacements in the molecule
Winiecka, Iwona,Dudkiewicz-Wilczynska, Jadwiga,Roman, Iza,Paruszewski, Ryszard
experimental part, p. 367 - 374 (2011/08/04)
A series of eight non-peptidic potential renin inhibitors have been designed and synthesized. All of them contain dipeptide replacement: (3S,4S)-4-amino-5-cyclohexyl-3-hydroxypentanoic acid (ACHPA) in their molecules. Four among them comprise two additional analogs of dipeptide: (3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid (AHPPA) and (3S,4S)-4-amino-3-hydroxy-6-methylheptanoic acid (statine, Sta). All of the synthesized compounds contain also hydrophobic portions to receive a moderate lipophilicity of the molecules. Inhibitory activity of the compounds was measured in vitro by HPLC determination of Leu-Val-Tyr-Ser released from the N-acetyltetradecapeptide substrate by renin in the presence of the inhibitor. Asp-α(OEt)-(S,S)-ACHPA-εAhx-Iaa (23) shows inhibitory activity (7%) at the concentration of 1.0 × 10-2 M. The other synthesized compounds show no inhibitory activity up to this concentration.
New renin inhibitors with pseudodipeptidic units in P1-P 1′ and P2′-P3′ positions
Paruszewski, Ryszard,Jaworski, Pawel,Winiecka, Iwona,Tautt, Jadwiga,Dudkiewicz, Jadwiga
, p. 850 - 853 (2007/10/03)
A series of four new potential renin inhibitors has been synthesized. The structure of the compounds was designed in such a way as to produce agents resistant to enzymatic degradation, metabolically stable, possibly potent and with improved oral absorptio
