Synthesis of New β-Amino Acids via 5-Oxazolidinones and the Arndt - Eistert Procedure

2005 ◽  
Vol 58 (11) ◽  
pp. 778 ◽  
Author(s):  
Andrew B. Hughes ◽  
Brad E. Sleebs
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Reductive Cleavage ◽  
High Yield ◽  
Amino Acid Derivatives ◽  
Peptide Therapeutics

N-Methyl β-amino acids are potentially useful amino acid derivatives for incorporation in lead peptide therapeutics. The syntheses of five such compounds are presented. Their synthesis via 6-oxazinanones was low yielding. Alternatively, reductive cleavage of a 5-oxazolidinone gave the N-methyl α-amino acid, which was then homologated via an Arndt–Eistert procedure in high yield to give the N-methyl β-amino acid.

scholarly journals Enantioselective synthesis of α-alkenyl α-amino acids via N–H insertion reactions

2016 ◽  
Vol 7 (2) ◽  
pp. 1104-1108 ◽  
Author(s):  
Jun-Xia Guo ◽  
Ting Zhou ◽  
Bin Xu ◽  
Shou-Fei Zhu ◽  
Qi-Lin Zhou
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Enantioselective Synthesis ◽  
Insertion Reaction ◽  
Amino Acid Derivatives ◽  
Insertion Reactions ◽  
Phosphoric Acids

A new highly enantioselective route to α-alkenyl α-amino acid derivatives using a N–H insertion reaction of vinyldiazoacetates and tert-butyl carbamate cooperatively catalyzed by achiral dirhodium(ii) carboxylates and chiral spiro phosphoric acids was developed.

Chiral sensors for determining the absolute configurations of α-amino acid derivatives

2018 ◽  
Vol 16 (37) ◽  
pp. 8311-8317 ◽  
Author(s):  
Zhongxiang Chen ◽  
Hongjun Fan ◽  
Shiwei Yang ◽  
Guangling Bian ◽  
Ling Song
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Derivatives ◽  
H Nmr ◽  
The Absolute

Two simple 1H NMR tests give the absolute configurations of α-amino acids.

scholarly journals Nitrosation and analysis of amino acid derivatives by isocratic HPLC

RSC Advances ◽  
2016 ◽  
Vol 6 (16) ◽  
pp. 13120-13128 ◽  
Author(s):  
Songül Ulusoy ◽  
Halil Ibrahim Ulusoy ◽  
Daniel Pleissner ◽  
Niels Thomas Eriksen
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Concentration ◽  
Amino Acid Concentration ◽  
Amino Acid Derivatives ◽  
Hydroxy Acids ◽  
Isocratic Hplc

Amino acids are transformed by nitrosation with dinitrogen trioxide into their corresponding α-hydroxy acids, which are separated and analysed by HPLC, and used to quantify the original amino acid concentration in samples.

scholarly journals Determination of Peptide Contact Points in the Human Angiotensin II Type I Receptor (AT1) with Photosensitive Analogs of Angiotensin II

1999 ◽  
Vol 13 (4) ◽  
pp. 578-586 ◽  
Author(s):  
Stéphane A. Laporte ◽  
Antony A. Boucard ◽  
Guy Servant ◽  
Gaétan Guillemette ◽  
Richard Leduc ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Angiotensin Ii ◽  
Transmembrane Domain ◽  
At1 Receptor ◽  
High Yield ◽  
Type I ◽  
Terminal Amino Acid ◽  
Contact Points ◽  
Terminal Amino

Abstract To identify ligand-binding domains of Angiotensin II (AngII) type 1 receptor (AT1), two different radiolabeled photoreactive AngII analogs were prepared by replacing either the first or the last amino acid of the octapeptide by p-benzoyl-l-phenylalanine (Bpa). High yield, specific labeling of the AT1 receptor was obtained with the 125I-[Sar1,Bpa8]AngII analog. Digestion of the covalent 125I-[Sar1,Bpa8]AngII-AT1 complex with V8 protease generated two major fragments of 15.8 kDa and 17.8 kDa, as determined by SDS-PAGE. Treatment of the[ Sar1,Bpa8]AngII-AT1 complex with cyanogen bromide produced a major fragment of 7.5 kDa which, upon further digestion with endoproteinase Lys-C, generated a fragment of 3.6 kDa. Since the 7.5-kDa fragment was sensitive to hydrolysis by 2-nitro-5-thiocyanobenzoic acid, we circumscribed the labeling site of 125I-[Sar1,Bpa8]AngII within amino acids 285 and 295 of the AT1 receptor. When the AT1 receptor was photolabeled with 125I-[Bpa1]AngII, a poor incorporation yield was obtained. Cleavage of the labeled receptor with endoproteinase Lys-C produced a glycopeptide of 31 kDa, which upon deglycosylation showed an apparent molecular mass of 7.5 kDa, delimiting the labeling site of 125I-[Bpa1]AngII within amino acids 147 and 199 of the AT1 receptor. CNBr digestion of the hAT1 I165M mutant receptor narrowed down the labeling site to the fragment 166–199. Taken together, these results indicate that the seventh transmembrane domain of the AT1 receptor interacts strongly with the C-terminal amino acid of[ Sar1, Bpa8]AngII, whereas the N-terminal amino acid of[ Bpa1]AngII interacts with the second extracellular loop of the AT1 receptor.

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