109772-33-0

Upstream product

• 41518-17-6 Z-Phe-O-COO-isoBu 
• 62-57-7 2-Aminoisobutyric acid 
• 501-53-1 benzyl chloroformate 
• 1161-13-3 N-Cbz-L-Phe 
• 63-91-2 L-phenylalanine 
• 98714-71-7 methyl 2-[((2S)-2-[[(benzyloxy)carbonyl]amino]-3-phenylpropanoyl)amino]-2-methylpropanoate 

Downstream Products

• 143868-68-2 Z-Phe-Aib-Trp-Aib-Trp-Glyol 
• 1161-13-3 N-Cbz-L-Phe 
• 62-57-7 2-Aminoisobutyric acid 
• 143868-66-0 Z-Trp-Aib-Phe-Aib-Trp-Aib-Trp-Glyol 
• 143868-65-9 H-Trp-Aib-Phe-Aib-Trp-Aib-Trp-Glyol 
• 143868-67-1 H-Phe-Aib-Trp-Aib-Trp-Glyol 

Relevant academic research and scientific papers

Synthesis of tripeptides containing heterocyclic α -amino acids by using heterospirocyclic 3-amino-2H-azirines

By using the 'azirine/oxazolone method', di- and tripeptides containing six-membered heterocyclic 4-amino-4-carboxylic acids with a piperidine, tetrahydropyran or tetrahydrothiopyran ring have been synthesized. It has been shown that the corresponding het

α-N-Protected dipeptide acids: A simple and efficient synthesis via the easily accessible mixed anhydride method using free amino acids in DMSO and tetrabutylammonium hydroxide

The importance of dipeptides both in medicinal and pharmacological fields is well documented and many efforts have been made to find simple and efficient methods for their synthesis. For this reason, we have investigated the synthesis of α-N-protected dipeptide acids by reacting the easily accessible mixed anhydride of α-N-protected amino acids with free amino acids under different reaction conditions. The combination of TBA-OH and DMSO has been found to be the best to overcome the low solubility of amino acids in organic solvents. Under these experimental conditions, the homogeneous phase condensation reaction occurs rapidly and without detectable epimerization. The present method is also applicable to side-chain unprotected Tyr, Trp, Glu, and Asp but not Lys. This latter residue is able to engage two molecules of mixed anhydride giving the corresponding isotripeptide. Moreover, the applicability of this protocol for the synthesis of tri- and tetrapeptides has been tested. This approach reduces the need for protecting groups, is cost effective, scalable, and yields dipeptide acids that can be used as building blocks in the synthesis of larger peptides.

Straightforward, racemization-free synthesis of peptides with fairly to very bulky di- and trisubstituted glycines

Several fully protected tri- and pentapeptides containing a central symmetrical α,α-dialkyl glycine residue, with the alkyl group varying from methyl or ethyl to benzyl, were synthesized in good yields by a strategy based on the Ugi-Passerini reaction. Ea

Influence of solvent viscosity on the rate of hydrolysis of dipeptides by carboxypeptidase Y

The influence of solvent viscosity on the rate of enzymatic hydrolysis of a series of dipeptides (Z-Phe-Gly, Z-Phe-Sar, Z-Phe-Ala, Z-Phe-NMeAla, Z-Phe-Aib and Z-Phe-Pro) by carboxypeptidase Y was investigated. The effect of solvent viscosity on the enzymatic hydrolysis revealed that whereas all Kcat values decreased with viscosity, those of the N-alkyl peptides decreased more than those of the N-H peptides. The kinetic behaviour implies the involvement of conformational changes of the enzyme in terms of the 'induced-fit' process. Copyright

Relationship between the hydrophobicity of dipeptides and the Michaelis-Menten constant Km of their hydrolysis by carboxypeptidase-Y and carboxypeptidase-A

The enzymatic hydrolysis of dipeptides by carboxypeptidase-Y and carboxypeptidase-A was investigated. In the enzymatic hydrolysis of the dipeptides, a good linear relationship (r = 0.997 and 0.999) was found between the Michaelis-Menten constant (Km) and the hydrophobicity of the substrates evaluated from relative elution volume in reversed-phase HPLC. The correlation suggests that the hydrophobicity of the C-terminal amino acid is a major factor in governing the stability of the enzyme-substrate complex. The difference in the slope of the linear-regression lines seems to reflect the degree of relative hydrophobicity of the binding pockets in carboxypeptidase-Y and carboxypeptidase-A.

Changes in Conformation and Antimicrobial Properties Caused by Replacement of D-Amino Acids with α-Aminoisobutyric Acid in the Gramicidin Backbone: Synthesis and Circular Dichroic Studies

In an attempt to mimic the stable helical structures of proteins with possible pore-forming ability in membranes, the linear gramicidin backbone has been changed by inserting achiral α-aminoisobutyric acids (Aib) in place of all of the alternatively seque

Selective Amide Cleavage in Peptides Containing α,α-Disubstituted α-Amino Acids

A new synthesis of dipeptides with terminal α,α-disubstituted α-amino acids, using 2,2-disubstituted 3-amino-2H-azirines 1 as amino-acid equivalents, is demonstrated.The reaction of 1 with N-protected amino acids leads to the corresponding dipeptide amide