178181-74-3

Upstream product

• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 104091-10-3 (R)-4-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-5-(benzyloxy)-5-oxopentanoic acid 
• 13030-09-6 1-benzyl L-glutamate 
• 122350-52-1 (4S)-5-benzyloxy-4-(9H-fluoren-9-ylmethoxycarbonylamino)-5-oxopentanoic acid 

Downstream Products

• 1298116-72-9 1-((9H-fluoren-9-yl)methyl) 2-benzyl (S)-pyrrolidine-1,2-dicarboxylate 
• 178181-75-4 (S)-5-[(3aS,4R,6R,7R,7aR)-4-(tert-Butyl-diphenyl-silanyloxymethyl)-7-hydroxy-2,2-dimethyl-tetrahydro-[1,3]dioxolo[4,5-c]pyran-6-yloxy]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-pentanoic acid benzyl ester 

Relevant academic research and scientific papers

Preparation of a glycopeptide analogue of type II collagen - Use of acid labile protective groups for carbohydrate moieties in solid phase synthesis of O-linked glycopeptides

A glycopeptide analogue of the immunodeficient T cell epitope on type II collagen has been prepared by solid phase synthesis. Preparation of a glycosylated amino acid from two monosaccharide units that carried silyl and isopropylidene protective groups and Fmoc 5-hydroxynorvaline was essential for the synthesis. After assembly of the glycopeptide the carbohydrate protective groups were removed simultaneously with acid catalyzed cleavage from the solid phase.

Total Synthesis of L-156,373 and an oxoPiz Analogue via a Submonomer Approach

The first chemical synthesis of L-156,373 (1), a potent oxytocin receptor antagonist isolated from Streptomyces silvensis, is reported. Assembly of the unusual d-Piz-l-Piz dipeptide subunit was achieved through a sequential electrophilic amination-acylati

ANTI-BACTERIAL PEPTIDE MACROCYCLES AND USE THEREOF

The present invention relates to compounds of formula (I) wherein X1 to X8 and R1 to R8 are as described herein, as well as pharmaceutically acceptable salts thereof for the use in the treatment or prevention of infections and resulting diseases caused by Pseudomonas aeruginosa.

Synthetic Approach to Argpyrimidine as a Tool for Investigating Nonenzymatic Posttranslational Modification of Proteins

Nonenzymatic posttranslational modifications (nPTMs) of proteins are involved in age-related, metabolic and other diseases and need to be investigated at the molecular level. Here, we describe how we used organic synthesis to enable the study of the effect of argpyrimidine (Apy), an nPTM that forms at arginine residues, on one of its target proteins. We developed an efficient approach to Apy as a universal building block for Fmoc-based solid-phase peptide synthesis that allows for the construction of peptides containing this nPTM in predetermined positions. Moreover, a straightforward one-step synthesis of protecting-group-free Apy was achieved, which enabled the preparation of gram-quantities of this noncanonical amino acid that can serve as a biomarker or a feedstock in construction of Apy-containing proteins via the expanded genetic code methods.

PEPTIDE MACROCYCLES AGAINST ACINETOBACTER BAUMANNII

The present invention provides compounds of formula (I) wherein X1 to X8 and R1 to R8 are as described herein, as well as pharmaceutically acceptable salts thereof. Further the present invention is concerned with the manufacture of the compounds of formula (I), pharmaceutical compositions comprising them and their use as medicaments for the treatment of diseases and infections caused by Acinetobacter baumannii.

Use of acid-labile protective groups for carbohydrate moieties in synthesis of glycopeptides related to type II collagen

β-D-Galactopyranosyl and α-D-glucopyranosyl-β-D-galactopyranosyl moieties carrying silyl, isopropylidene and 4-methoxybenzyl protective groups have been attached to the amino acid 5-hydroxy-L-norvaline. The resulting glycosylated building blocks were used in Fmoc solid-phase synthesis of glycopeptides related to a fragment from type II collagen which is immunodominant in a mouse model for rheumatoid arthritis. The protective groups used for the carbohydrate moieties were completely removed during acid catalyzed cleavage of the glycopeptides from the solid phase under conditions which left the O-glycosidic bonds intact.