959991-45-8

Upstream product

• 3417-91-2 L-tyrosine methyl ester HCl 
• 4326-36-7 (S)-N-(tert-butoxycarbonyl)tyrosine methyl ester 
• 109-64-8 1,3-dibromo-propane 
• 938195-80-3 methyl N-(2,6-dichlorobenzoyl)-L-tyrosinate 
• 627-18-9 1-bromo-3-propanol 

Downstream Products

• 959991-46-9 methyl N-(tert-butoxycarbonyl)-O-{3-[(tert-butoxycarbonyl)(pyridin-2-yl)amino]propyl}-L-tyrosinate 
• 953788-33-5 3-iodopropyl-Boc-Tyr 
• 1174388-74-9 methyl O-[3-(pyridin-2-ylamino)propyl]-L-tyrosinate hydrochloride 

Relevant academic research and scientific papers

Synthesis and incorporation of unnatural amino acids to probe and optimize protein bioconjugations

The utilization of unnatural amino acids (UAAs) in bioconjugations is ideal due to their ability to confer a degree of bioorthogonality and specificity. In order to elucidate optimal conditions for the preparation of bioconjugates with UAAs, we synthesized 9 UAAs with variable methylene tethers (2-4) and either an azide, alkyne, or halide functional group. All 9 UAAs were then incorporated into green fluorescent protein (GFP) using a promiscuous aminoacyl-tRNA synthetase. The different bioconjugations were then analyzed for optimal tether length via reaction with either a fluorophore or a derivatized resin. Interestingly, the optimal tether length was found to be dependent on the type of reaction. Overall, these findings provide a better understanding of various parameters that can be optimized for the efficient preparation of bioconjugates.

Proximity-enabled protein crosslinking through genetically encoding haloalkane unnatural amino acids

The selective generation of covalent bonds between and within proteins would provide new avenues for studying protein function and engineering proteins with new properties. New covalent bonds were genetically introduced into proteins by enabling an unnatural amino acid (Uaa) to selectively react with a proximal natural residue. This proximity-enabled bioreactivity was expanded to a series of haloalkane Uaas. Orthogonal tRNA/synthetase pairs were evolved to incorporate these Uaas, which only form a covalent thioether bond with cysteine when positioned in close proximity. By using the Uaa and cysteine, spontaneous covalent bond formation was demonstrated between an affibody and its substrate Z protein, thereby leading to irreversible binding, and within the affibody to increase its thermostability. This strategy of proximity-enabled protein crosslinking (PEPC) may be generally expanded to target different natural amino acids, thus providing diversity and flexibility in covalent bond formation for protein research and protein engineering. Copyright

N-(BENZOYL)-O- [2- (PYRIDIN- 2 -YLAMINO) ETHYL] -L-TYROSINE DERIVATIVES AND RELATED COMPOUNDS AS A5B1 ANTAGONISTS FOR THE TREATMENT OF SOLID TUMORS

The present invention relates to compounds that inhibit of a5b1 function, processes for their preparation, pharmaceutical compositions containing them as the active ingredient, to their use as medicaments and to their use in the manufacture of medicaments for use in the treatment in warm-blooded animals such as humans of diseases that have a significant angiogenesis or vascular component such as for treatment of solid tumours. The present invention also relates to a5b1 antagonists that also exhibit appropriate selectivity profile(s) against other integrins.