93710-17-9

Upstream product

• 35661-39-3 N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 35661-38-2 Fmoc-alanine 
• 128369-71-1 (S)-methyl-(N-allyloxycarbonyl)phenylalaninate 
• 142061-92-5 N-(9-fluorenylmethoxycarbonyl)-L-alanyl fluoride 
• 103321-50-2 9H-fluoren-9-ylmethyl [(1S)-2-chloro-1-methyl-oxoethyl]carbamate 
• 1158245-85-2 (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)propanethioic S-acid 
• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 
• 86060-86-8 (9H-fluoren-9-yl-methoxy)carbonyl-L-alanine pentafluorophenyl ester 

Downstream Products

• 218785-75-2 Fmoc-L-Ala-L-Phe-OH 
• 1361509-98-9 (S)-methyl 2-((S)-2-((S)-2-(benzyloxycarbonylamino)-4-methylpentanamido)propaneselenoamido)-3-phenylpropanoate 
• 1361509-54-7 (S)-methyl 2-((S)-2-(((9H-fluoren-9-yl)methoxy)carbonylamino)propaneselenoamido)-3-phenylpropanoate 

Relevant academic research and scientific papers

Synthesis of Dipeptide, Amide, and Ester without Racemization by Oxalyl Chloride and Catalytic Triphenylphosphine Oxide

An efficient triphenylphosphine oxide-catalyzed amidation and esterification for the rapid synthesis of a series of dipeptides, amides, and esters is described. This reaction is applicable to challenging couplings of hindered carboxylic acids with weakly

Liquid Phase Peptide Synthesis via One-Pot Nanostar Sieving (PEPSTAR)

Herein, a one-pot liquid phase peptide synthesis featuring iterative addition of amino acids to a “nanostar” support, with organic solvent nanofiltration (OSN) for isolation of the growing peptide after each synthesis cycle is reported. A cycle consists of coupling, Fmoc removal, then sieving out of the reaction by-products via nanofiltration in a reactor-separator, or synthesizer apparatus where no phase or material transfers are required between cycles. The three-armed and monodisperse nanostar facilitates both efficient nanofiltration and real-time reaction monitoring of each process cycle. This enabled the synthesis of peptides more efficiently while retaining the full benefits of liquid phase synthesis. PEPSTAR was validated initially with the synthesis of enkephalin-like model penta- and decapeptides, then octreotate amide and finally octreotate. The crude purities compared favorably to vendor produced samples from solid phase synthesis.

Fast Amide Couplings in Water: Extraction, Column Chromatography, and Crystallization Not Required

In the micelle of PS-750-M, the presence of 3° amides from the surfactant proline linker mimics dimethylformamide, dimethylacetamide, and N-methyl-2-pyrrolidone. The resultant micellar properties enable extremely fast amide couplings mediated by 1-ethyl-3

Iterative design of a biomimetic catalyst for amino acid thioester condensation

Herein, the design of a catalyst that combines lessons learned from peptide biosynthesis, enzymes, and organocatalysts is described. The catalyst features a urea scaffold for carbonyl recognition and elements of nucleophilic catalysis. In the presence of 10 mol % of the organocatalyst, the rate of peptide bond formation is accelerated by 10000-fold over the uncatalyzed reaction between Fmoc-amino acid thioesters and amino acid methyl esters.

Iodine-Mediated Oxidative Coupling of Hydroxamic Acids with Amines towards a New Peptide-Bond Formation

An efficient and straightforward approach for the coupling of Nα-protected hydroxamic acids with an amino component in the presence of iodine is delineated. The reaction is mediated by the formation of unstable but reactive acyl nitroso intermediates. The peptide hydroxamic acids were found to be useful substrates in coupling reactions.

Synthesis of selenoxo peptides and oligoselenoxo peptides employing LiAlHSeH

Synthesis of selenoxo peptides by the treatment of Nα- protected peptide esters with a combination of PCl5 and LiAlHSeH is delineated. The method is simple, high-yielding, and free from racemization. Thus obtained selenoxo peptides are used as units for N-terminal chain extension through Nα-deprotection/coupling to yield peptide-selenoxo peptide hybrids. Multiple selenation is demonstrated by conversion of two peptide bonds of tripeptides into selenoxo peptide bonds. Amino acid derived arylamides are also converted into aryl selenoamides. C6H 5-CSeNH-Val-OMe 8f is obtained as single crystal, and its structure was determined through X-ray diffraction study.

The method of preparation of enantiomerically enriched products of condensation from racemic acids or acids of the low enentiomeric purity

The method of obtaining enantiomerically enriched condensation products consists of subjecting a racemic acid or an acid of low enantiomeric purity to the action of a condensing reagent - a chiral N-triazinylammonium tetrafluoroborate (formula 1), a chira

Characterization of Nα-Fmoc-protected dipeptide isomers by electrospray ionization tandem mass spectrometry (ESI-MSn): Effect of protecting group on fragmentation of dipeptides

A series of positional isomeric pairs of Fmoc-protected dipeptides, Fmoc-Gly-Xxx-OY/Fmoc-Xxx-Gly-OY (Xxx = Ala, Val, Leu, Phe) and Fmoc-Ala-Xxx-OY/Fmoc-Xxx-Ala-OY (Xxx = Leu, Phe) (Fmoc = [(9-fluorenylmethyl) oxy]carbonyl) and Y = CH3/H), have been characterized and differentiated by both positive and negative ion electrospray ionization ion-trap tandem mass spectrometry (ESI-IT-MSn). In contrast to the behavior of reported unprotected dipeptide isomers which mainly produce y 1+ and/or a1+ ions, the protonated Fmoc-Xxx-Gly-OY, Fmoc-Ala-Xxx-OY and Fmoc-Xxx-Ala-OY yield significant b 1+ ions. These ions are formed, presumably with stable protonated aziridinone structures. However, the peptides with Gly- at the N-terminus do not form b1+ ions. The [M + H]+ ions of all the peptides undergo a McLafferty-type rearrangement followed by loss of CO2 to form [M + H-Fmoc + H]+. The MS3 collision-induced dissociation (CID) of these ions helps distinguish the pairs of isomeric dipeptides studied in this work. Further, negative ion MS 3 CID has also been found to be useful for differentiating these isomeric peptide acids. The MS3 of [M-H-Fmoc + H]- of isomeric peptide acids produce c1-, z1 - and y1- ions. Thus the present study of Fmoc-protected peptides provides additional information on mass spectral characterization of the dipeptides and distinguishes the positional isomers. Copyright

Facile amide formation via S -nitrosothioacids

Here we report a novel amide bond formation strategy from simple thioacid and amine starting materials. The reaction is mediated by unstable but very reactive S-nitrosothioacid intermediates. This fast reaction under mild conditions should be useful in synthesis.(Figure Presented)