17528-16-4

Upstream product

• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 
• 53558-76-2 Boc-(phenylalanyl)4-OMe 
• 17528-19-7 N-alpha-carbobenzoxy-L-phenylalanyl-L-phenylalanyl-L-phenylalanine methyl ester 
• 13082-29-6 L-phenylalanyl-L-phenylalanine methyl ester 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 

Downstream Products

• 65757-10-0 L-phenylalanyl-L-phenylalanyl-L-phenylalanyl-L-phenylalanyl-L-phenylalanine 

Relevant academic research and scientific papers

Thio-Bromo “Click” Reaction Derived Polymer–Peptide Conjugates for Their Self-Assembled Fibrillar Nanostructures

The synthesis and self-assembly of peptide–polymer conjugates into fibrillar nanostructures are reported, based on the amyloidogenic peptide KLVFF. A strategy for rational synthesis of polymer–peptide conjugates is documented via tethering of the amyloidogenic peptide segment LVFF (Aβ17-20) and its modified derivative FFFF to the hydrophilic poly(ethylene glycol) monomethyl ether (mPEG) polymer via thio-bromo based “click” chemistry. The resultant conjugates mPEG-LVFF-OMe and mPEG-FFFF-OMe are purified via preparative gel permeation chromatography technique (with a yield of 61% and 64%, respectively), and are successfully characterized via combination of spectroscopic and chromatographic methods, including electrospray ionization time-of-flight mass spectrometry. The peptide-guided self-assembling behavior of the as-constructed amphiphilic supramolecular materials is further investigated via transmission electron microscopic and circular dichroism spectroscopic analysis, exhibiting fibrillar nanostructure formation in binary aqueous solution mixture.

Chloride-Assisted Peptide Macrocyclization

The role of the Cl- anion as a templating agent for the synthesis of cyclopeptides was assessed through the preparation of three new homocyclolysines and other six cyclic peptides by head-to-tail lactamization. Isolated yields of products obtai

Peptide bond formation by aminolysin-A catalysis: A simple approach to enzymatic synthesis of diverse short oligopeptides and biologically active puromycins

A new S9 family aminopeptidase derived from the actinobacterial thermophile Acidothermus cellulolyticus was cloned and engineered into a transaminopeptidase by site-directed mutagenesis of catalytic Ser491 into Cys. The engineered biocatalyst, designated aminolysin-A, can catalyze the formation of peptide bonds to give linear homo-oligopeptides, hetero-dipeptides, and cyclic dipeptides using cost-effective substrates in a one-pot reaction. Aminolysin-A can recognize several C-terminal-modified amino acids, including the l- and d-forms, as acyl donors as well as free amines, including amino acids and puromycin aminonucleoside, as acyl acceptors. The absence of amino acid esters prevents the formation of peptides; therefore, the reaction mechanism involves aminolysis and not a reverse reaction of hydrolysis. The aminolysin system will be a beneficial tool for the preparation of structurally diverse peptide mimetics by a simple approach.