109924-24-5

Upstream product

• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 6011-14-9 2-aminoacetonitrile hydrochloride 
• 151-63-3 cyanomethylamine sulfate 
• 518314-53-9 2-(N-(tert-butoxycarbonyl)amino)-2-benzylpropanedioic diethyl ester 
• 102831-44-7 diethyl tert-butoxycarbonylaminomalonate 
• 100-39-0 benzyl bromide 
• 3674-06-4 Boc-Phe-ONSu 

Downstream Products

• 90374-41-7 (+)-N-(tert-Butoxycarbonyl)-L-phenylalanyl-glycin-thioamid 
• 191033-19-9 (S)-tert-butyl (1-((1-cyanocyclopropyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 710350-64-4 L-phenylalanyl-glycine-nitrile 
• 191033-34-8 benzyl (S)-(1-((1-cyanocyclopropyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 191033-48-4 N-Cbz-(S)-phenylalanine-(S)-cyclopropanecarboxylic acid methyl ester 
• 109924-32-5 N-(tert-Butoxycarbonyl)-L-phenylalanyl-glycin-imidthiosaeure-S-ethylester 
• 42428-77-3 acetonitrile 

Relevant academic research and scientific papers

Influence of azide incorporation on binding affinity by small papain inhibitors

In order to develop affinity-based biosensor platforms, appropriate ligands with a functional handle for immobilization onto a biosensor surface are required. To this end, a library of papain inhibitors was designed and synthesized, containing different a

Experimental study and computational modelling of cruzain cysteine protease inhibition by dipeptidyl nitriles

Chagas disease affects millions of people in Latin America. This disease is caused by the protozoan parasite Trypanossoma cruzi. The cysteine protease cruzain is a key enzyme for the survival and propagation of this parasite lifecycle. Nitrile-based inhib

Nitrile-containing enzyme inhibitors and ruthenium complexes thereof

The invention provides nitrile-containing protease inhibitors caged to ruthenium compounds. The nitrile-caged ruthenium compounds provide inactivated inhibitors that can be delivered to surface or site for activation, for example, but exposure to light. The invention also provides methods for delivering protease inhibitors to subjects for the therapeutic treatment of conditions such as cancer.

PROTEASE INHIBITORS

A peptidyl nitrile of the general formula (I) or a pharmaceutically acceptable salt or prodrug thereof, is capable of selectively inhibiting dipeptidyl-peptidase I (DPP-I), also known as cathepsin C. A compound of the invention is useful as an active subs

CATHEPSIN CYSTEINE PROTEASE INHIBITORS AND THEIR USE

The present invention relates to compounds and compositions for treating diseases associated with cysteine protease activity. The compounds are reversible inhibitors of cysteine proteases S, K, F, L and B. Of particular interest are diseases associated with Cathepsin S. In addition this invention also discloses processes for the preparation of such inhibitors.

Identification of dipeptidyl nitriles as potent and selective inhibitors of cathepsin B through structure-based drug design

Cathepsin B is a member of the papain superfamily of cysteine proteases and has been implicated in the pathology of numerous diseases, including arthritis and cancer. As part of an effort to identify potent, reversible inhibitors of this protease, we examined a series of dipeptidyl nitriles, starting with the previously reported Cbz-Phe-NH-CH2CN (19, IC50 = 62 μM). High-resolution X-ray crystallographic data and molecular modeling were used to optimize the P1, P2, and P3 substituents of this template. Cathepsin B is unique in its class in that it contains a carboxylate recognition site in the S2′ pocket of the active site. Inhibitor potency and selectivity were enhanced by tethering a carboxylate functionality from the carbon α to the nitrile to interact with this region of the enzyme. This resulted in the identification of compound 10, a 7 nM inhibitor of cathepsin B, with excellent selectivity over other cysteine cathepsins.

Direct dialkylation of peptide nitriles. Application to the synthesis of 1-aminocyclopropane-1-carboxylic acid (Acc)-containing dipeptides

Several 1-aminocyclopropane-1-carboxylic acid-containing dipeptides (Acc-CP) have been prepared by regioselective dialkylation of peptoids containing α-aminonitriles as C-terminal residues.Regioselective deprotonation of the aminomethylene center using a

130. Poly(dipeptamidinium) Salts: Definition and Methods of Preparation

Poly(dipeptamidines) are polypeptide derivatives in which the carbonyl oxygen of each second backbone amide group is replaced by an imine nitrogen (see A).So far, such derivatives have been unknown.Polyprotonated salts of them (= poly(dipeptamidinium) salts) are of interest in view of their intrinsic constitutional relationship to the structure of polynucleotides: the number of covalent bonds between neighboring centers of positive charge in poly(dipeptamidinum) salts is identical to the number of covalent bonds between neighboring centers of negative charge in natural polynucleotides (see D).Poly(dipeptamidinium) polycations and polynucleotide polyanions are constitutionally and electrostatically complementary structures.Since poly(dipeptamidines) are (formally) polymers of dipeptide nitriles, and, since they can be expected to give polypeptides on hydrolysis, the relationship mentioned above deserves attention and experimental study in context with the problem of designing chemical models of biogenesis.This paper describes methods for the chemical preparation, the spectral characterization, and some chemical properties of homodipeptidic poly(dipeptamidinium) salts in the L-alanyl-glycyl and L-phenylalanyl-glycyl series.The methods of preparation include a stepwise construction of defined lower oligomers (up to hexamer) as weel as, in the L-alanyl-glycyl series, a one-preparation poly-condensation procedure leading to polymers containing an average of ca. 20 dipeptamidinium units (Schemes 4,6 and 7).