34337-45-6

Upstream product

• 72156-62-8 N^α-(tert-butoxycarbonyl)-L-tryptophyl-L-phenylalanine methyl ester 
• 63-91-2 L-phenylalanine 
• 3392-11-8 2,5-dioxopyrrolidin-1-yl N-(tert-butoxycarbonyl)-L-tryptophanate 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 13139-14-5 Boc-Trp-OH 

Downstream Products

• 709666-38-6 N-[1-[1-(2-benzyloxycarbonylamino-1-(S)-carbamoyl-ethylcarbamoyl)-2-(S)-phenyl-ethylcarbamoyl]-2-(S)-(1H-indol-3-yl)-ethyl]-succinamic acid 
• 709665-35-0 H-Trp-Phe-Dpr(Z)-NH₂ 
• 709666-41-1 N-[1-[1-(2-amino-1-(S)-carbamoyl-ethylcarbamoyl)-2-(S)-phenyl-ethylcarbamoyl]-2-(S)-(1H-indol-3-yl)-ethyl]-succinamic acid 
• 709665-34-9 Boc-Trp-Phe-Dpr(Z)-NH₂ 

Relevant academic research and scientific papers

Epimerization-Free C-Term Activation of Peptide Fragments by Ball Milling

Peptides were produced in high yields and, if any, very low epimerization, by mechanochemical coupling of peptide fragments containing highly epimerization-prone and/or highly hindered amino acids at C-term. Ball milling was clearly identified as the key element enabling one to obtain such results.

INHIBITORS OF GROWTH FACTOR ACTIVATION ENZYMES

The present invention generally relates to compounds that are useful for inhibiting one or more of hepatocyte growth factor activator, matriptase, hepsin, Factor Xa, or thrombin. The present invention also relates to various methods of using the inhibitor compounds including treating a malignancy, a pre-malignant condition, or cancer by administering an effective amount of the inhibitor to a subject in need thereof.

Epimerization-free C-terminal peptide activation

Smooth operation: C-terminal peptide activation with full stereointegrity was accomplished using a copper(II)-mediated coupling reaction of carboxylic acids with arylboroxines (see scheme, NCL = native chemical ligation, Boc = tert-butoxycarbonyl). This method allows epimerization-free activation and ligation of peptides with racemization-prone phenylglycine at the C terminus.

Antimicrobial activity, biocompatibility and hydrogelation ability of dipeptide-based amphiphiles

The development of new antibiotics is of increasing importance due to the growing resistance power of microbes against conventional drugs. To this end, cationic peptides are emerging as clinically potent antimicrobial agents. In the present study, we have