156939-64-9

Upstream product

• 103321-53-5 (S)-(9H-fluoren-9-yl)methyl 1-chloro-3-methyl-1-oxobutan-2-ylcarbamate 
• 160885-98-3 2-[(S)-(fluoren-9-ylmethoxycarbonyl)amino]-3-methylbutan-1-ol 
• 227624-28-4 Fmoc-Val-N(CH₃)-OCH₃ 
• 68858-20-8 Fmoc-Val-OH 
• 84890-99-3 Fmoc-Val-O-COO-isoBu 

Downstream Products

• 851976-94-8 1-{1-[(1-benzyl-2-fluoro-2-phenylsulfanyl-ethyl-amino)-methyl]-2-methyl-propylamino}-2-{[(9H-fluoren-9-ylmethoxy)-hydroxymethyl]-amino}-ethanol 
• 851976-67-5 2-amino-1-{1-[(1-benzyl-2-fluoro-2-phenylsulfanyl-ethyl-amino)-methyl]-2-methyl-propylamino}-ethanol 
• 851976-93-7 N¹-(1-benzyl-2-fluoro-2-phenylsulfanyl-ethyl)-3-methyl-butane-1,2-diamine 
• 439685-27-5 [(S)-1-isopropyl-4-oxo-6-(toluene-4-sulfonyl)hex-2-enyl]carbamic acid 9H-fluoren-9-ylmethyl ester 

Relevant academic research and scientific papers

Formation of bis (Fmoc-amino ethyl)-N-glycine derivatives by reductive amination of Fmoc-amino aldehydes with NaBH3CN

Unexpected results of the reductive amination of Fmoc-amino aldehydes by NaBH3CN are described. From glycine and Fmoc-4-t-Butoxy-tyrosinal, a small amount of double condensation product was obtained beside the initially desired product Fmoc-Tyr(OtBu)-ψ(CH2NH)-Gly-OH. From glycine methyl ester and Fmoc-glycinal, we only recovered the reduced peptide bond isostere, but from glycine and Fmoc-glycinal, bis(Fmoc-amino ethyl)-N-glycine was obtained as a major product.

Distinct Lugdunins from a New Efficient Synthesis and Broad Exploitation of Its MRSA-Antimicrobial Structure

A new solid-phase peptide synthesis and bioprofiling of the antimicrobial activity of lugdunin, a fibupeptide, enable a comprehensive structure-activity relationship (SAR) study (MRSA Staphylococcus aureus). Distinct lugdunin analogues with variation of the three important amino acids Val2, Trp3, and Leu4 are readily available based on the established high-output synthesis. This efficient synthesis concept takes advantage of the presynthesized thiazolidine building block. To gain further knowledge of SAR, d-Val2, and d-Leu4 were replaced with aliphatic amino acids. For l-Trp3 derivatization, a set of non-natural aromatic amino acids with manifold substitution and annulation patterns precisely shows structural imperatives, starting from the exchange of d-Val6 → d-Trp6 with a 2-fold improved biological activity. d-Trp6-lugdunin analogues with additional variation of d-Val2 and d-Leu4 residues were designed and synthesized followed by antimicrobial profiling. For the first time, these SAR studies deliver valuable information on the tolerance of other amino acids to d-Val2, l-Trp3, and d-Leu4 in the sequence of lugdunin.

Synthesis and biological activity of peptide α-ketoamide derivatives as proteasome inhibitors

Proteasome activity affects cell cycle progression as well as the immune response, and it is largely recognized as an attractive pharmacological target for potential therapies against several diseases. Herein we present the synthesis of a series of pseudo

Discovery of a novel class of potent HCV NS4B inhibitors: SAR studies on piperazinone derivatives

HTS screening identified compound 2a (piperazinone derivative) as a low micromolar HCV genotype 1 (GT-1) inhibitor. Resistance mapping studies suggested that this piperazinone chemotype targets the HCV nonstructural protein NS4B. Extensive SAR studies were performed around 2a and the amide function and the C-3/C-6 cis stereochemistry of the piperazinone core were essential for HCV activity. A 10-fold increase in GT-1 potency was observed when the chiral phenylcyclopropyl amide side chain of 2a was replaced with p- fluorophenylisoxazole-carbonyl moiety (67). Replacing the C-6 nonpolar hydrophobic moiety of 67 with a phenyl moiety (95) did not diminish the GT-1 potency. A heterocyclic thiophene moiety (103) and an isoxazole moiety (108) were incorporated as isosteric replacements for the C-6 phenyl moiety (95), resulting in significant improvement in GT-1b and 1a potency. However, the piperazonone class of compounds lacks GT-2 activity and, consequently, were not pursued further into development.

A direct and efficient stereoconservative procedure for the selective oxidation of N-protected β-amino alcohols

An efficient, very simple and eco-friendly procedure has been developed for the synthesis of highly enantioenriched α-amino aldehydes by IBX-mediated oxidation of the corresponding β-amino alcohols. The procedure has been applied to a wide range of substr

Nonionic side chains modulate the affinity and specificity of binding between functionalized polyamines and structured RNA

This Communication introduces side-chain-bearing polyamines as molecules for selective recognition of folded RNA structures. The complex folded structures associated with RNA create binding pockets for proteins, and also binding sites for small molecules.

Solid-phase synthesis of peptide vinyl sulfones as potential inhibitors and activity-based probes of cysteine proteases

(Matrix presented) Peptide vinyl sulfones were prepared from 2-chlorotrityl resin-bound phenolic amino vinyl sulfones in high yield and purity. This method enables the convenient synthesis of peptide vinyl sulfones having different amino acids at the Psu

An Ionic Liquid Mediated Efficient Oxidation of Alcohols Using o-Iodoxybenzoic Acid (IBX) - A Simple and Eco-friendly Protocol

An environmentally benign ionic liquid is shown to be for the first time an excellent medium for mild and selective oxidation of alcohols using IBX at room temperature.

Small ring constrained peptidomimetics. Synthesis of epoxy peptidomimetics, inhibitors of cysteine proteases

Different dipeptide analogues containing an oxirane ring in the place of the peptidic bond were prepared starting from naturally occurring amino acids. N-Fmoc-amino aldehydes were transformed into the corresponding methoxyvinyl derivatives through a Wittig reaction, and the addition of PhSeCl gave a series of different α-phenylselenyl aldehydes. Mukajiama reaction with silylketene acetals gave an intermediate product that was finally transformed into the desired oxiranyl peptidomimetics. Following this strategy we were able to control three new contiguous stereocenters starting from the enantiomerically pure amino acid. The dipeptide analogues could be used in SPPS on a SASRIN resin as the final epoxides were relatively unstable under acidic conditions. Moreover the synthesis of the single dipeptide mimetics was carried out on solid phase to generate a small library of epoxy peptidomimetics. Some of the products prepared in this work resulted as time-dependent reversible inhibitors of cysteine protease.

Synthesis of 9-fluorenylmethoxycarbonyl-protected amino aldehydes

9-Fluorenylmethoxycarbonyl-protected amino aldehydes could be efficiently prepared in good yields by using two methods: (i) NaBH4 reduction of Fmoc-protected mixed anhydrides, followed by the Swern oxidation of the alcohols; and (ii) LiAlH