1384472-59-6

Upstream product

• 60-18-4 L-tyrosine 
• 70930-22-2 Phe-Tyr methyl ester trifluoroacetate 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 3417-91-2 L-tyrosine methyl ester HCl 
• 66076-54-8 N-tert-butyloxycarbonyl-L-phenylalanine-L-tyrosine methyl ester 
• 1080-06-4 L-Tyr-OMe 
• 13122-90-2 Boc-Phe-Phe-OH 
• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 
• 24424-99-5 di-tert-butyl dicarbonate 
• 63-91-2 L-phenylalanine 

Relevant academic research and scientific papers

Photo-induced charge-transfer complex formation and organogelation by a tripeptide

A terminally protected tripeptide Boc-Phe-Phe-Tyr-OMe 1 and picric acid form a photo induced charge-transfer complex and organogels. The interactions between stacked aromatic units play a key role in the assembly process. UV light (366 nm) has been used a

Transition-metal ion-mediated morphological transformation of pyridine-based peptide nanostructures

Inspired by natural metallopeptides, we have rationally designed two pyridine-conjugated short peptides. These two peptide conjugates formed a pair of constitutional isomers that helped us describe their structure-function relationship. Both the isomers consisted of an equal number of aromatic amino acid residues, but shuffling was observed in the position of two key amino acids, viz; tyrosine and phenylalanine, which brought a remarkable change in their self-assembling behavior. The presence of specific functional groups and chemical diversity in both conjugates made them very active towards metal coordination. Both the constitutional isomers adopted different pathways of self-assembly, which could be further controlled or transformed by the use of transition metal ions. Interestingly, it was observed that the metal ions could precisely control the morphology of these metallopeptide nanostructures and make them more stable. Therefore, such artificial metallopeptides possess remarkable advantages over the natural counterparts primarily due to their tailor-made chemical structures.