97216-17-6 Usage
Description
(2S)-N-(2-naphthyl)pyrrolidine-2-carboxamide hydrobromide is a chiral pyrrolidine derivative that belongs to the class of chemical compounds known as hydrobromide salts. As a chiral molecule, it has an enantiomer, (2R)-N-(2-naphthyl)pyrrolidine-2-carboxamide hydrobromide. (2S)-N-(2-naphthyl)pyrrolidine-2-carboxamide hydrobromide is frequently utilized in pharmaceutical research as a fundamental building block for the synthesis of a variety of biologically active molecules.
Uses
Used in Pharmaceutical Research:
(2S)-N-(2-naphthyl)pyrrolidine-2-carboxamide hydrobromide is used as a key intermediate in the synthesis of biologically active compounds, playing a crucial role in drug discovery and development. Its unique structure and properties make it a valuable component in creating new pharmaceutical agents.
Used in Neuroscience and Medicinal Chemistry:
(2S)-N-(2-naphthyl)pyrrolidine-2-carboxamide hydrobromide is particularly relevant in the fields of neuroscience and medicinal chemistry, where it is employed for the development of drugs targeting the central nervous system. Its potential applications in these areas highlight its importance in creating treatments for neurological disorders and other related conditions.
Used in Laboratory Settings:
The hydrobromide salt form of (2S)-N-(2-naphthyl)pyrrolidine-2-carboxamide enhances its solubility and stability, making it more manageable and practical for use in laboratory research. This improved handling and usability facilitate its incorporation into various experimental procedures and chemical reactions.
Check Digit Verification of cas no
The CAS Registry Mumber 97216-17-6 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 9,7,2,1 and 6 respectively; the second part has 2 digits, 1 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 97216-17:
(7*9)+(6*7)+(5*2)+(4*1)+(3*6)+(2*1)+(1*7)=146
146 % 10 = 6
So 97216-17-6 is a valid CAS Registry Number.
97216-17-6Relevant articles and documents
POST-PROLINE ENDOPEPTIDASE. PARTIAL PURIFICATION AND CHARACTERIZATION OF THE ENZYME FROM PIG KIDNEYS
Hauzer, Karel,Servitova, Linda,Barth, Tomislav,Jost, Karel
, p. 1139 - 1148 (2007/10/02)
Post-proline endopeptidase was isolated from pig kidneys and partially purified.The procedure consisted of fractionation with ammonium sulphate, ion exchange chromatography on DEAE-Sephadex A-50, gel filtration on Sephadex G-200 and rechromatography on DEAE-Sephadex A-50.The preparation had 55 times higher specific activity than the crude extract and did not contain any contaminating enzymic activities.The enzyme cleaved a number of proline-containing peptides and was strictly specific in catalyzing the hydrolysis of the peptide bond on the carboxyl side of the proline residue.The optimum pH for the hydrolysis of the synthetic peptides benzyloxycarbonylglycyl-prolyl-leucyl-glycinamide and benzyloxycarbonyl-glycyl-proline β-naphthylamide was 7.8-8.0 and, in the case of benzyloxycarbonylglycyl-proline p-nitroanilide, 7.2 to 7.5.For the hydrolysis of the tetrapeptide benzyloxycarbonylglycyl-prolyl-leucyl-glycinamide, the Km value of 75 μmol l-1 was obtained.
