47507-41-5

Upstream product

• 72-18-4 L-valine 
• 51987-73-6 (S)-2-tert-butoxycarbonylamino-3-phenyl-propionic acid methyl ester 
• 2754-02-1 N-(N-(1,1-dimethylethoxycarbonyl)-L-phenylalanyl)-L-valine methyl ester 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 6306-52-1 L-valine methylester hydrochloride 
• 68858-20-8 Fmoc-Val-OH 
• 17498-50-9 L-valine hydrochloride 
• 119153-87-6 (C₅H₉O₂)C₉H₉NO(O)(CO₂C₂H₅) 
• 21760-98-5 L-valine benzyl ester 
• 4070-48-8 L-Valine methyl ester 
• 136282-23-0 benzyl (tert-butoxycarbonyl)-L-phenylalanyl-L-valinate 
• 3674-06-4 Boc-Phe-ONSu 

Downstream Products

• 175444-54-9 Boc-Phe-Val-Phe-Thr(Bn)-Leu-OBn 
• 945265-22-5 Boc-Phe-Val-Pro-OMe 
• 403852-47-1 H-Phe-Val-Phe-Thr(Bn)-Leu-OBn 
• 150854-44-7 H-Ile-Leu-Gly-Phe-Val-Phe-Thr-Leu-OH 
• 403852-49-3 Boc-Ile-Leu-Gly-Phe-Val-Phe-Thr(Bn)-Leu-OBn 
• 403852-50-6 N-[β-D-(glucopyranuronic acid)-3-nitrobenzyloxycarbonyl]-Gly-Ile-Leu-Gly-Phe-Val-Phe-Thr-Leu-OH 
• 403852-44-8 methyl N-[β-D-glucopyranuronate-3-nitrobenzyloxycarbonyl]-Gly-Ile-Leu-Gly-Phe-Val-Phe-Thr-Leu-OH 
• 1446422-77-0 C₃₁H₅₄N₃O₈P 
• 1446422-78-1 C₃₁H₅₄N₃O₈P 
• 1446422-80-5 C₃₀H₅₂N₃O₈P 

Relevant academic research and scientific papers

SULFOXONIUM YLIDE DERIVATIVES AS PROBES FOR CYSTEINE PROTEASE

The present invention relates to compounds of formula I bearing a sulfoxonium ylide moiety as warhead, or salts thereof. Such compounds can be used as activity-based probes for cysteine proteases such as cathepsin X, in methods of detecting cysteine protease activity and in related diagnostic or therapeutic methods.

Photoredox-Mediated Reaction of gem-Diborylalkenes: Reactivity Toward Diverse 1,1-Bisborylalkanes

The use of gem-diborylalkenes as radical-reactive groups is explored for the first time. These reactions provide an efficient and general method for the photochemical conversion of gem-diborylalkenes to rapidly access 1,1-bisborylalkanes. This method expl

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.

Convenient peptide synthesis without protection of C-Terminals

Condensation of carboxylic acids 1 and 5 with unprotected α-amino acids 2 via activation by ethyl chloroformate and triethylamine proceeded effectively to afford the corresponding amides in 5099% yields. Tripeptide 7c was obtained in 42% yield from the dipeptide 6c in a similar manner.

Design, synthesis and primary activity assay of bi- or tri-peptide analogues with the scaffold l-arginine as amino-peptidase N/CD13 inhibitors

A series of bi- or tri-peptide analogues with the scaffold l-arginine were designed, synthesized and evaluated for their inhibitory activities against amino-peptidase N (APN) and metalloproteinase-2 (MMP-2). The primary activity assay showed that all the compounds exhibited higher inhibitory activities against APN than MMP-2. Within this series, compounds C6 and C7 (IC50 = 4.2 and 4.3 μM) showed comparable APN inhibitory activities with the positive control bestatin (IC50 = 3.8 μM).

Design and synthesis of a novel class of furan-based molecules as potential 20S proteasome inhibitors

A novel class of furan-based compounds as potential 20S proteasome inhibitors have been designed and synthesized, among which nine compounds are peptide derivatives and six molecules are statine peptidomimetics. The C-terminal furanyl moiety was introduced to target molecules as furan-based amino acids. All the compounds were obtained steadily with moderate to high yield. Compound 12 was a selective moderate potent proteasome peptidomimetic inhibitor. It inhibited HepG2 and HL-60 proliferation effectively.

Synthetic approaches to peptides containing the l-Gln-l-Val-D(S)-Dmt motif

The pseudoprolines S-Dmo (5,5-dimethyl-4-oxaproline) and R-Dmt (5,5-dimethyl-4-thiaproline) have been used to study the effects of forcing a fully cis conformation in peptides. Synthesis of peptides containing these (which have the same configuration as l-Pro) is straightforward. However, synthesis of peptides containing S-Dmt is difficult, owing to the rapid cyclisation of l-Aaa-S-Dmt amides and esters to form the corresponding diketopiperazines (DKP); thus the intermediacy of l-Aaa-S-Dmt amides and esters must be avoided in the synthetic sequence. Peptides containing the l-Gln-l-Val-D(S)-Dmt motif are particularly difficult, owing to the insolubility of coupling partners containing Gln. Introduction of Gln as N-Boc-pyroglutamate overcame the latter difficulty and the dipeptide active ester BocPygValOC6F5 coupled in good yield with S-DmtOH. BocPygVal-S- DmtNH(CH2)2C6H4NO2 was converted quantitatively to BocGlnVal-S-DmtNH(CH2)2C6H4NO2 with ammonia, demonstrating the utility of this approach. Two peptide derivatives (CbzSerLysLeuGlnVal-S-DmtNH(CH2)2C6H4NO2 and CbzSerSerLysLeuGlnVal-S- DmtNH(CH2)2C6H4NO2) were assembled, using these new methods of coupling a dipeptide acid active ester with S-DmtOH and introduction of Gln as Pyg, followed by conventional peptide couplings. The presence of the Val caused these peptides to be cleaved very slowly by prostate-specific antigen (PSA) at Leu ↓ Gln, rather than the expected Gln ↓ Val.

The role of terminal tyrosine residues in the formation of tripeptide nanotubes: a crystallographic insight

Terminally protected acyclic tripeptides containing tyrosine residues at both termini self-assemble into nanotubes in crystals through various non-covalent interactions including intermolecular hydrogen bonds. The nanotube has an average internal diameter of 5 ? (0.5 nm) and the tubular ensemble is developed through the hydrogen-bonded phenolic-OH side chains of tyrosine (Tyr) residues [Org. Lett. 2004, 6, 4463]. We have synthesized and studied several tripeptides 3-6 to probe the role of tyrosine residues in nanotube structure formation. These peptides either have only one Tyr residue at N- or C-termini or they have one or two terminally located phenylalanine (Phe) residues. These tripeptides failed to form any kind of nanotubular structure in the solid state. Single crystal X-ray diffraction studies of these peptides 3-6 clearly demonstrate that substitution of any one of the terminal Tyr residues in the Boc-Tyr-X-Tyr-OMe (X=Val or Ile) sequence disrupts the formation of the nanotubular structure indicating that the presence of two terminally located Tyr residues is vital for nanotube formation.

Synthesis and biological activity of the prodrug of class I major histocompatibility peptide GILGFVFTL activated by β-glucuronidase

The first synthesis of a prodrug of HLA-A2.1 associated antigenic influenza peptide 2a was accomplished. Two methods for synthesis of prodrugs of antigenic peptides activated by β-glucuronidase and comprising a self-immolative 3-nitrobenzyloxycarbonyl moiety were investigated. Reaction of β-glucuronic acid glycoside of 4-hydroxy-3-nitrobenzyl alcohol (3) with N,N′-disuccinimidyl carbonate (DSC) followed by conjugation with AlaOMe, Gly, Thr, Phe-Leu, and Leu-Arg gave carbamates 4a-4f. Deacetylation of 4b and 4e with MeONa/MeOH gave β-glucuronides 5b and 5e. Compound 5e was converted to β-glucuronic acid conjugate 6e by the action of pig liver esterase (PLE). Compound 6e is a substrate for β-glucuronidase. Method of a direct introduction of the prodrug residue into antigenic nonapeptide GILGFVFTL (2b) failed. Alternately, glycine conjugate 5b was activated to pentafluorophenyl ester 10. Model coupling of 10 with Phe-Leu gave tripeptide conjugate ester 11a which was hydrolyzed by PLE to uronic acid 12. Condensation of 10 with octapeptide ILGFVFTL (9) gave prodrug precursor 11b. Octapeptide 9 was prepared by de novo synthesis using a racemization-free fragment coupling method. Ester hydrolysis with Ba(OH)2/MeOH gave the target prodrug 2a which is a substrate for β-glucuronidase. Prodrug 2a does not bind to HLA-A2.1 of T2 human cells defective in major histocompatibility complex I (MHC I)-associated peptide processing. Addition of β-glucuronidase restored the binding to the level observed with parent nonapeptide 2b although higher concentrations of prodrug 2a and enzyme were necessary.

Application of AlMe3-mediated amidation reactions to solution phase peptide synthesis

A practical modification of the Weinreb amidation protocol employing amino acids as the amine reaction partner has been developed that allows for the facile synthesis of oligopeptides in solution.