33294-55-2

Upstream product

• 13734-41-3 N-Boc-(S/R)-valine 
• 538-75-0 dicyclohexyl-carbodiimide 
• 13734-41-3 t-Boc-L-valine 
• 6306-52-1 L-valine methylester hydrochloride 
• 77867-79-9 2-tert-butoxy-4-isopropyl-L-5(4H)-oxazolone 

Downstream Products

• 72155-67-0 N-(tert-butoxycarbonyl)-L-valyl-4(S)-amino-3(S)-hydroxy-5-phenylpentanoyl-L-alanyl isoamylamide 
• 84850-92-0 N-(tert-butyloxycarbonyl)-L-valyl-4(S)-amino-3(S)-hydroxy-6-methylheptanoyl-L-alanyl-L-phenylalanine methyl ester 
• 89028-20-6 N-<(tert-butoxycarbonyl)-L-valyl>-(2R,4R,5S)-5-amino-1-(benzyloxy)-2,7-dimethyloctan-4-ol 
• 89103-67-3 N-<(tert-butoxycarbonyl)-L-valyl>-(2R,4S,5S)-5-amino-1-(benzyloxy)-2,7-dimethyloctan-4-ol 
• 105943-61-1 N-<(tert-butyloxycarbonyl)-L-valyl>-(2R,4RS,5S)-5-amino-2-benzyl-1-(benzyloxy)-7-methyloctan-4-ol 
• 105562-88-7 N-(tert-butyloxycarbonyl)-L-valyl-N⁷-benzyl-N⁷-(benzyloxycarbonyl)-4(S),7-diamino-3(R,S)-hydroxyheptanoic acid ethyl ester 
• 105562-89-8 N-(tert-butyloxycarbonyl)-L-valyl-L-valyl-N⁷-benzyl-N⁷-(benzyloxycarbonyl)-4(S),7-diamino-3(R,S)-hydroxyheptanoic acid ethyl ester 
• 105617-27-4 N-(tert-butyloxycarbonyl)-L-valyl-L-valyl-N⁸-(benzyloxycarbonyl)-4(S),8-diamino-3(R)-hydroxyoctanoic acid ethyl ester 
• 105562-72-9 N-(tert-butyloxycarbonyl)-L-valyl-L-valyl-N⁸-(benzyloxycarbonyl)-4(S),8-diamino-3(S)-hydroxyoctanoic acid ethyl ester 
• 105617-26-3 N-(tert-butyloxycarbonyl)-L-valyl-N⁸-(benzyloxycarbonyl)-4(S),8-diamino-3(R)-hydroxyoctanoic acid ethyl ester 
• 105562-71-8 N-(tert-butyloxycarbonyl)-L-valyl-N⁸-(benzyloxycarbonyl)-4(S),8-diamino-3(S)-hydroxyoctanoic acid ethyl ester 
• 93279-10-8 Z-D-Ser(N-Boc-L-Val)-OTce 
• 502421-44-5 Boc-L-valacyclovir 
• 130619-10-2 N^α-t-butyloxycarbonyl-L-valyl-L-asparginyl-L-phenylalanyl hydrazide 

Relevant academic research and scientific papers

Expeditious, potentially primordial, aminoacylation of nucleotides

(Chemical Equation Presented) In the beginning: Mixed carboxylic phosphoric anhydrides 3, formed from 3′-nucleotides 1 and amino acid N-carboxyanhydrides 2, undergo competing rearrangement to 2′-aminoacyl esters 4 and cyclization to 2′,3′-cyclic phosphates 5. The intramolecular aminoacyl transfer is faster than the cyclization despite the ease with which 2′,3′-cyclic phosphates are formed through any other form of phosphate activation.

Synthesis and characterization of novel dipeptide ester prodrugs of acyclovir.

Four dipeptide (Gly-Gly, Gly-Val, Val-Val, Val-Gly) ester prodrugs of 9-[(2-hydroxyethoxy)methyl]guanine (acyclovir, ACV) were synthesized. LC/MS was used to characterize the new prodrugs. Both 1H NMR and 13C NMR spectra of the four prodrugs of ACV were measured and assigned based on spectral comparison with compounds of similar structures.

MERTK DEGRADERS AND USES THEREOF

The present invention provides compounds, compositions thereof, and methods of using the same.

Synthesis of amino-acid derivatives of chrysin

Various conjugates of amino acids with chrysin in which the amino acid was bonded through the C- or N-terminus to the flavone were prepared using peptide chemistry methods (symmetric anhydrides and activated esters).

Induced axial chirality in the biphenyl core of the proatropoisomeric, Cα-tetrasubstituted α-amino acid residue Bip in peptides

An induced axial chirality in the biphenyl core of the 2′,1′:1,2;1″,2″:3,4-dibenzcyclohepta-1, 3-diene-6-amino-6-carboxylic acid (Bip) residue, a conformationally labile, atropoisomeric, Cα-tetrasubstituted α-amino acid, was observed by CD and 1H NMR spectroscopic techniques in the linear dipeptides Boc-Bip-Xaa*-OMe where Boc = tert-butoxycarbonyl, OMe = methoxy, and Xaa* = D- and/or L-Ala, -Val, -Leu, -Phe, -(αMe)Val and -(αMe)Leu. Chiral induction was significantly lower in the isomeric dipeptides Boc-Xaa*-Bip-OMe, with the Xaa* residue located at the N-terminus of Bip, as well as in the cyclic dipeptide cyclo-[Bip-L-Ala]. The results obtained in solution were confirmed by X-ray diffraction analysis of a crystalline sample of Boc-(R)-Bip-D-Ala-OMe.

Amino acid derivatives of 2-R-7-hydroxy-3',4'-ethylenedioxyisoflavones

A number of 7-O-aminoacyl derivatives of isoflavones have been obtained by the interaction of 2-R-7-hydroxy-3′,4′-ethylenedioxyisoflavones with the symmetrical anhydrides of N-protected amino acids.

Periplanetin CC-1 Myotropic Peptide from corpora cardiaca of Cockroach Periplaneta americana L. New Synthesis and Biological Studies

Periplanetin CC-1 (Glu-Val-Asn-Phe-Ser-Pro-Asn-Trp-NH2) (1) neuropeptide from corpora cardiaca of the American cocroach Periplaneta americana has been synthesized by the liquid-phase method.In biological studies on the larvae of yellow mealworm, Tenebrio

Synthetic studies on quinoxaline antibiotics. III. Synthesis of nortriostin A, a triostin A analog lacking N-methyl groups on the cystine and valine residues

Nortriostin A, which is an analog of a cyclic octadepsipeptide antibiotic triostin A and contains one cystine and two valine residues substituted for the N,N'-dimethylcystine and N-methylvaline residues of the antibiotic, was synthesized with Z-D-Ser[Boc-Ala-Cys(MeBzl)-Val]-OH and Z-D-Ser[H-Ala-Cys(MeBZ)-Val]-OTce as key intermediates. The synthetic analog showed no antimicrobial activity at a concentration of 100 μg/ml and was found to exist as a single structure in solution as examined by 1H-NMR spectroscopy. The latter observation suggests that the conformer equilibrium known to occur with triostin A is a consequence of the presence of N-methyl peptide bonds in the antibiotic molecule. Nortriostin A, which is an analog of a cyclic octadepsipeptide antibiotic triostin A and contains one cystine and two valine residues substituted for the N,N prime -dimethylcystine and N-methylvaline residues of the antibiotic, was synthesized with Z-//D-Ser left bracket Boc-Ala-Cys(MeBzl)-Val right bracket -OH and Z-//D-Ser left bracket H-Ala-Cys(MeBzl)-Val right bracket -OTce as key intermediates. The synthetic analog showed no antimicrobial activity at a concentration of 100 mu g/ml and was found to exist as a single structure in solution as examined by **1H-NMR spectroscopy. The latter observation suggests that the conformer equilibrium known to occur with triostin A is a consequence of the presence of N-methyl peptide bonds in the antibiotic molecule.

Synthesis of Analogues of the Carboxyl Protease Inhibitor Pepstatin. Effect of Structure in Subsite P3 on Inhibition of Pepsin

A series of pepstatin analogues having minimum structural requirements for tight-binding inhibition has been synthesized and tested on porcine pepsin.Subtle changes in the geometry and size of side chains at the valine-1 position of pepstatin were found to dramatically affect inhibitor potency as well as the type of kinetic behavior observed.The inhibitors reported here can be grouped into two categories: the more potent inhibitors are slow-binding inhibitors, i.e., exhibit slow, time-dependent inhibition; the weaker inhibitors, with Ki values greater than 10-8M, are not time-dependent inhibitors.A minimum kinetic mechanism is proposed to account for the observed kinetic behavior.