alanyl-alanyl-alanine and glycylsarcosine

alanyl-alanyl-alanine has been researched along with glycylsarcosine* in 1 studies

Other Studies

1 other study(ies) available for alanyl-alanyl-alanine and glycylsarcosine

Article	Year
Recognition of 2-aminothiazole-4-acetic acid derivatives by the peptide transporters PEPT1 and PEPT2. European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences, 2007, Volume: 32, Issue:1 The H(+)/peptide cotransporters PEPT1 and PEPT2 have gained considerable interest in pharmaceutical sciences as routes for drug delivery. It is, therefore, of interest to develop uncommon artificial substrates for the two carriers. This study was initiated to investigate the binding affinity of 2-aminothiazole-4-acetic acid (ATAA) conjugates with amino acids to PEPT1 and PEPT2. The 2-aminothiazole-4-acetic acid derivatives have been synthesised and tested for their affinity to PEPT1 and PEPT2. The K(i) values were compared with in silico predicted values from CoMSIA models. C-terminal ATAA-Xaa conjugates proved to be low to medium inhibitors of the [(14)C]Gly-Sar uptake at both carrier systems whereas N-terminal Xaa-ATAA conjugates exhibited medium to high affinity. A promising candidate for further functionalisation is Val-ATAA which shows extraordinary high affinity to PEPT1. Topics: Amino Acids; Animals; Anti-Bacterial Agents; Biological Transport; Caco-2 Cells; Ceftibuten; Cells, Cultured; Cephalosporins; Dipeptides; Humans; Kidney Tubules, Proximal; Kinetics; Models, Molecular; Molecular Structure; Oligopeptides; Peptide Transporter 1; Protein Binding; Rats; Symporters	2007

Article

Year

Recognition of 2-aminothiazole-4-acetic acid derivatives by the peptide transporters PEPT1 and PEPT2.

European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences, 2007, Volume: 32, Issue:1

The H(+)/peptide cotransporters PEPT1 and PEPT2 have gained considerable interest in pharmaceutical sciences as routes for drug delivery. It is, therefore, of interest to develop uncommon artificial substrates for the two carriers. This study was initiated to investigate the binding affinity of 2-aminothiazole-4-acetic acid (ATAA) conjugates with amino acids to PEPT1 and PEPT2. The 2-aminothiazole-4-acetic acid derivatives have been synthesised and tested for their affinity to PEPT1 and PEPT2. The K(i) values were compared with in silico predicted values from CoMSIA models. C-terminal ATAA-Xaa conjugates proved to be low to medium inhibitors of the [(14)C]Gly-Sar uptake at both carrier systems whereas N-terminal Xaa-ATAA conjugates exhibited medium to high affinity. A promising candidate for further functionalisation is Val-ATAA which shows extraordinary high affinity to PEPT1.

Topics: Amino Acids; Animals; Anti-Bacterial Agents; Biological Transport; Caco-2 Cells; Ceftibuten; Cells, Cultured; Cephalosporins; Dipeptides; Humans; Kidney Tubules, Proximal; Kinetics; Models, Molecular; Molecular Structure; Oligopeptides; Peptide Transporter 1; Protein Binding; Rats; Symporters

2007