New Amino Acids for the Topographical Control of Peptide Conformation: Synthesis of All the Isomers of .alpha.,.beta.-Dimethylphenylalanine and .alpha.,.beta.-Dimethyl-1,2,3,4-tetrahydroisoquinoline-3-carboxylic Acid of High Optical Purity

1994 ◽  
Vol 59 (7) ◽  
pp. 1789-1795 ◽  
Author(s):  
Wieslaw M. Kazmierski ◽  
Zofia Urbanczyk-Lipkowska ◽  
Victor J. Hruby
Keyword(s):  
Amino Acids ◽  
Carboxylic Acid ◽  
Optical Purity ◽  
Peptide Conformation ◽  
High Optical Purity ◽  
Alpha Beta

Nitrilases Catalyze Key Step to Conformationally Constrained GABA Analogous γ-Amino Acids in High Optical Purity

2007 ◽  
Vol 72 (19) ◽  
pp. 7423-7426 ◽  
Author(s):  
Margit Winkler ◽  
Astrid C. Knall ◽  
Martin R. Kulterer ◽  
Norbert Klempier
Keyword(s):  
Amino Acids ◽  
Optical Purity ◽  
Conformationally Constrained ◽  
High Optical Purity

scholarly journals The T Cell Receptor (TRB) Locus in Tursiops truncatus: From Sequence to Structure of the Alpha/Beta Heterodimer in the Human/Dolphin Comparison

Genes ◽  
2021 ◽  
Vol 12 (4) ◽  
pp. 571
Author(s):  
Giovanna Linguiti ◽  
Sofia Kossida ◽  
Ciro Leonardo Pierri ◽  
Joumana Jabado-Michaloud ◽  
Geraldine Folch ◽  
...  
Keyword(s):  
Amino Acids ◽  
T Cell ◽  
T Cell Receptor ◽  
Tursiops Truncatus ◽  
Cell Receptor ◽  
Sequence Alignments ◽  
T Cell Receptor Beta ◽  
Alpha Beta ◽  
Receptor Beta ◽  
Complementarity Determining Region

The bottlenose dolphin (Tursiops truncatus) belongs to the Cetartiodactyla and, similarly to other cetaceans, represents the most successful mammalian colonization of the aquatic environment. Here we report a genomic, evolutionary, and expression study of T. truncatus T cell receptor beta (TRB) genes. Although the organization of the dolphin TRB locus is similar to that of the other artiodactyl species, with three in tandem D-J-C clusters located at its 3′ end, its uniqueness is given by the reduction of the total length due essentially to the absence of duplications and to the deletions that have drastically reduced the number of the germline TRBV genes. We have analyzed the relevant mature transcripts from two subjects. The simultaneous availability of rearranged T cell receptor α (TRA) and TRB cDNA from the peripheral blood of one of the two specimens, and the human/dolphin amino acids multi-sequence alignments, allowed us to calculate the most likely interactions at the protein interface between the alpha/beta heterodimer in complex with major histocompatibility class I (MH1) protein. Interacting amino acids located in the complementarity-determining region according to IMGT numbering (CDR-IMGT) of the dolphin variable V-alpha and beta domains were identified. According to comparative modelization, the atom pair contact sites analysis between the human MH1 grove (G) domains and the T cell receptor (TR) V domains confirms conservation of the structure of the dolphin TR/pMH.

Synthesis and Antibacterial Potency of 4-Methyl-2,7-dioxo-1,2,3,4,7,10- hexahydropyrido[2,3-ƒ]quinoxaline-8-carboxylic acid, Selected [a]-Fused Heterocyles and Acyclic Precursors

2007 ◽  
Vol 62 (11) ◽  
pp. 1453-1458 ◽  
Author(s):  
Yusuf M. Al-Hiari ◽  
Ali M. Qaisia ◽  
Mohammad Y.Abu Shuheil ◽  
Mustafa M. El-Abadelah ◽  
Wolfgang Voelter
Keyword(s):  
Amino Acids ◽  
Carboxylic Acid ◽  
Antibacterial Activities ◽  
Sodium Dithionite ◽  
E Coli ◽  
Pipecolinic Acid

The reaction of 7-chloro-1-cyclopropyl-6-fluoro-8-nitro-4-oxo-1,4-dihydroquinoline-3-carboxylic acid (7) with each of sarcosine and (±)-pipecolinic acid afforded the corresponding N-(4- oxoquinolin-7-yl)-α-amino acids 8 and 9. Reductive lactamization of the latter with sodium dithionite gave hexahydropyrido[2,3- f ]quinoxaline (10) and octahydrodipyrido[1,2-a : 2,3- f ]quinoxaline (11) derivatives, respectively. Compounds 8 - 11 and their homologs 1 - 6, accessible from (S)-proline, (2S, 4R)-4-hydroxyproline and (S)-tetrahydroisoquinoline-3-carboxylic acid exhibit good to excellent antibacterial activities against E. coli and S. aureus.

The Use of Chiral Recognition in a Bioorganic System for Determination of Optical Purity of Labelled Amino Acids

2010 ◽  
Vol 91 (5) ◽  
pp. 491-491
Author(s):  
G. Bergson ◽  
C. Halldin ◽  
H. Lundqvist ◽  
B. Långström ◽  
M. Malmqvist
Keyword(s):  
Amino Acids ◽  
Chiral Recognition ◽  
Optical Purity
Sign in / Sign up

Export Citation Format

Share Document