23262-07-9

Upstream product

• 3082-75-5 L-Alanine ethyl ester 
• 15050-24-5 N-(benzyloxycarbonyl)glycyl chloride 
• 5680-83-1 N-(benzyloxycarbonyl)glycine hydrazide 
• 79002-45-2 N-benzyloxycarbonyl-glycine 
• 1115-59-9 (S)-alanine ethyl ester hydrochloride 
• 87023-85-6 1-(Cbz-glycyl)-3,5-dimethylpyrazole 
• 125412-51-3 (2S,3S)-S-(N-carbobenzyloxyglycyl)-S'-L-alanyl-2,3-bis(4-mercapto-2-oxabutyl)-1,4,7,10,13,16-hexaoxacyclooctadecane hydrochloride 
• 501-53-1 benzyl chloroformate 
• 1138-80-3 N-(Benzyloxycarbonyl)glycine 
• 1145-81-9 ethyl 2-(benzyloxycarbonylamino)ethanoate 

Downstream Products

• 3079-63-8 (S)-2-(2-Benzyloxycarbonylamino-acetylamino)-propionic acid 
• 23404-17-3 benzyloxycarbonylglycyl-alanine hydrazide 
• 908577-37-7 N-(N-hippuroyl-L-alanyl)-L-leucine hydrazide 
• 62686-56-0 N-[N-(N-benzyloxycarbonyl-glycyl)-L-alanyl]-L-leucine hydrazide 
• 62686-52-6 Z-Gly-L-Ala-L-Leu-OMe 
• 616861-80-4 HSalGly-L-AlaOEt 
• 5854-09-1 salicylglycyl-L-alanine 

Relevant academic research and scientific papers

Interaction of VIVO, VVO2 and CuII with a peptide analogue SalGly-L-Ala

The formation of complexes of a tripeptide analogue, salicylglycyl-L-alanine [HOC6H4C(O)NHCH2C(O)NHCH(CH3) -COOH, H2SalGly-L-Ala], was studied with CuII, VIVO and VVO2 in aqueous solution using pH-potentiometric and spectroscopic (UV/Vis, CD, EPR and 51V NMR) techniques. The results demonstrated the ambidentate character of the ligand. The metal ion-induced deprotonation and subsequent coordination of the two neighbouring amide groups was shown to occur in a cooperative way in the pH range 5-6. At pH ≈ 6.5 a complex with an (O-, 2 x CON-, COO-) binding set becomes predominant for both CuII, and VIVO. The affinity of the phenolate-O- for VIVO is high and the ligand is bound to this metal ion even at pH values greater than 10. Conversely, the affinity for VVO2 is significantly lower and no interaction between this metal oxo-ion and the ligand could be detected in the pH range 2-12. In contrast, with the dipeptide analogue H2SalGly, chelation involving the deprotonated amide-N-could be unambiguously detected. Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2003.

New system for peptide synthesis using N-acylpyrazoles

New system of peptide synthesis was described. The extension of one amino acid unit on the peptide chain was constituted from only 2 reaction steps, the conversion from esters to the corresponding N-acylpyrazoles and the subsequent aminolysis with amino esters. This new system was distinctive from the conventional peptide synthesis, which was consisted of 3 steps of the deprotection, the activation and the condensation. Moreover, the key intermediate N-acylpyrazoles exhibited the excellent properties of high sensitivity and separability for the chiral column on HPLC using the UV detector.

Biomimetic studies using artificial systems. IV. Biomimetic peptide synthesis by using multifunctionalized crown ethers as a novel enzyme model. A new concept in mimicking of enzyme-catalyzed bond-forming reactions.

A novel approach to the mimicking of enzyme-catalyzed bond-forming reactions has been examined using multifunctionalized chiral crown ethers. In addition to the 18-crown-6 moiety as a binding site, the host have one thiol and one thio ester with an N-prot