166655-48-7

Upstream product

• 54613-99-9 Boc-(S)-Lys(2-Cl-Z)-OH 

Downstream Products

• 166655-75-0 [2-tert-butoxycarbonylamino-6-(2-chloro-benzyloxycarbonylamino)-hexylamino]-acetic acid methyl ester 
• 871815-68-8 (S)-2-[(S)-2-tert-Butoxycarbonylamino-6-(2-chloro-benzyloxycarbonylamino)-hexylamino]-6-(2-chloro-benzyloxycarbonylamino)-hexanoic acid 
• 871815-70-2 (R)-2-[(S)-2-tert-Butoxycarbonylamino-6-(2-chloro-benzyloxycarbonylamino)-hexylamino]-6-(2-chloro-benzyloxycarbonylamino)-hexanoic acid 
• 871815-72-4 [2-tert-butoxycarbonylamino-6-(2-chloro-benzyloxycarbonylamino)-hexylamino]-acetic acid 
• 871815-64-4 (R)-2-[(S)-2-tert-Butoxycarbonylamino-6-(2-chloro-benzyloxycarbonylamino)-hexylamino]-6-(2-chloro-benzyloxycarbonylamino)-hexanoic acid methyl ester 
• 871815-62-2 (S)-2-[(S)-2-tert-Butoxycarbonylamino-6-(2-chloro-benzyloxycarbonylamino)-hexylamino]-6-(2-chloro-benzyloxycarbonylamino)-hexanoic acid methyl ester 
• 1229593-84-3 C₂₅H₄₀ClN₃O₆ 
• 1229593-83-2 C₃₃H₄₉ClN₆O₈S 

Relevant academic research and scientific papers

Design and Synthesis of Activity-Based Probes and Inhibitors for Bleomycin Hydrolase

Summary Bleomycin hydrolase (BLMH) is a neutral cysteine aminopeptidase that has been ascribed roles in many physiological and pathological processes, yet its primary biological function remains enigmatic. In this work, we describe the results of screening of a library of fluorogenic substrates to identify non-natural amino acids that are optimally recognized by BLMH. This screen identified several substrates with kcat/KM values that are substantially improved over the previously reported fluorogenic substrates for this enzyme. The substrate sequences were used to design activity-based probes that showed potent labeling of recombinant BLMH as well as endogenously expressed BLMH in cell extracts, and in intact cells. Importantly, we identify potent BLMH inhibitors that are able to fully inhibit endogenous BLMH activity in intact cells. These probes and inhibitors will be valuable new reagents to study BLMH function in cellular and animal models of human diseases where BLMH is likely to be involved.

Synthesis of new chiral PNAs bearing a dipeptide-mimic monomer with two lysine-derived stereogenic centres

The synthesis of new chiral PNA analogues based on lysine is reported. In particular, l- and/or d-lysine-based PNA submonomers bearing two lysine side chains exactly spaced as in the dipeptide Lys-Lys were synthesized and incorporated in the middle of dec

Synthesis of chiral vinylogous sulfonamidopeptides (vs-peptides)

Chiral vinylogous amino sulfonic acids (vs-amino acids) were synthesized starting from either L- or D-α-amino acids via N-Boc-α-amino aldehydes. Wittig-Horner reaction with methyl (or ethyl) diethylphosphoryl methanesulfonate and nBuLi gave the corresponding α,β-unsaturated sulfonates in high yield and complete (E) stereoselectivity. Cleavage of the methyl (ethyl) ester was effected by treatment of the sulfonates with nBu4NI in refluxing acetone. Treatment of the nBu4N+ sulfonate salts with SO2Cl2/PPh3/CH2Cl2 gave the corresponding sulfonyl chlorides as stable chromatographable compounds. The synthetic sequence proved successful not only starting from α-amino acids carrying unfunctionalized side-chains (Ala, Val, Phe, Leu, Pro), but also with functionalized α-amino acids (Ser, Tyr, Gln) provided that the side chains were suitably protected. The sulfonyl chlorides were coupled with the amine salts to give vs-dipeptides. Amine hydrochlorides were prepared from N-Boc derivatives by treatment with HCl in methanol or ethyl acetate. The process was further iterated to give vstripeptides and vs-tetrapeptides. The above procedure was also used to synthesize "mixed" peptides, which incorporate both proteinogenic α-amino acids and vs-amino acids. Proteinogenic α-amino acids were incorporated at both the C-terminal and the N-terminal position.