18670-98-9

Upstream product

• 15761-38-3 L-N-Boc-Ala 
• 42854-62-6 L-alanine benzyl ester p-toluenesulfonate 
• 17831-01-5 H-Ala-OBzl 
• 5557-81-3 L-alanine benzyl ester hydrochloride 
• 133039-96-0 (S)-(1-fluoro-1-oxoprop-2-yl)carbamic acid tert-butyl ester 
• 126400-95-1 N-(tert-butoxycarbonyl)-L-alanine benzyl ester 

Downstream Products

• 27317-69-7 N-tert-butoxycarbonyl-L-alanyl-L-alanine 
• 69871-83-6 L-alanyl-L-alanine benzyl ester hydrochloride 
• 82748-55-8 L-alanyl-L-alanine benzyl ester trifluoroacetate 
• 18671-06-2 N-t-butoxycarbonyl-L-alanyl-L-alanyl-L-alanine benzyl ester 
• 77935-62-7 H-L-Ala-L-Ala-L-Ala-OBzl_.HCl 
• 77935-61-6 Boc-Tea-L-Ala-L-Ala-OBzl 
• 766460-08-6 Boc-Tea-L-Ala-L-Ala-L-Ala-OBzl 
• 77935-67-2 H-Tea-L-Ala-L-Ala-L-Ala-OBzl_.HCl 
• 82748-54-7 Ala-Ala-O-benzyl 
• 129149-42-4 Boc-pyrAla-Ala₂-OBzl 
• 132645-46-6 Boc-dmaPhe-Ala₂-OBzl 
• 132645-47-7 Boc-dmaPhe-Ala₂-OH 
• 111334-31-7 H-Ser(Bzl)-Ser-Thr-Ser-Ala-Ala-OBzl 
• 111334-29-3 Boc-Ser(Bzl)-Ser-Thr-Ser-Ala-Ala-OBzl 

Relevant academic research and scientific papers

Functionalized oligoanthranilamides: Modular and conformationally controlled scaffolds

This paper describes the use of functionalize oligoanthranilamides as conformationally controlle scaffolds for molecular recognition. Oligomers of anthranilamides are stabilize by the formation of intramolecular six-membere hydrogen bonds in a linear strand conformation. Onto alternate anthranilic aci units, we have attached di- or tripeptide recognition units with the potential to form intramolecular hydrogen bonds to an intercalated peptide strand . Using 1H NMR dilution experiments in CDCl3, we have observe chemical shift changes that are consistent with the formation of an extended hydrogen bondes sheet dimer. We also demonstrate that the bis-alanine functionalize strands are able to form discrete hydrogen bonded complexes with dipeptide substrates an to bind hexanoyl alanylalanine selectively over its benzyl ester. In the presence of excess hydrogen bon donors and acceptors, the oligoanthranilamide strand retained its linear conformation, pointing to the potential of this modular design as a useful and stable scaffold for molecular recognition studies. Copyright

Peptide Synthesis in Fluorinated Alcohols Mixed with Proton Accepting Partners

1,1,1,3,3,3-Hexafluoro-2-propanol is an excellent dissolver of protected oligopeptides but a barren medium for the condensation reaction of peptides.The solvent, however, could be changed to help the reaction proceed by mixing with a proton accepting solv

Rapid and column-free syntheses of acyl fluorides and peptides usingex situgenerated thionyl fluoride

Thionyl fluoride (SOF2) was first isolated in 1896, but there have been less than 10 subsequent reports of its use as a reagent for organic synthesis. This is partly due to a lack of facile, lab-scale methods for its generation. Herein we report a novel protocol for theex situgeneration of SOF2and subsequent demonstration of its ability to access both aliphatic and aromatic acyl fluorides in 55-98% isolated yields under mild conditions and short reaction times. We further demonstrate its aptitude in amino acid couplings, with a one-pot, column-free strategy that affords the corresponding dipeptides in 65-97% isolated yields with minimal to no epimerization. The broad scope allows for a wide range of protecting groups and both natural and unnatural amino acids. Finally, we demonstrated that this new method can be used in sequential liquid phase peptide synthesis (LPPS) to afford tri-, tetra-, penta-, and decapeptides in 14-88% yields without the need for column chromatography. We also demonstrated that this new method is amenable to solid phase peptide synthesis (SPPS), affording di- and pentapeptides in 80-98% yields.

Glycopeptide derivatives for the preservation and protection of biological materials and microorganisms

The present invention relates to a compound of the following formula (I): in which at least one and only one group chosen among R5, R6 and R7 is a group of the following formula: The present invention relates also to uses

One-pot mechanosynthesis of aromatic amides and dipeptides from carboxylic acids and amines

Environmentally friendly one-pot synthesis of amides, bis-amides and dipeptides by mechanochemical carbodiimide-mediated coupling of carboxylic acids and amines is described; high reaction yields and simple aqueous work-up allow for the clean, practical and fast preparation of a variety of compounds containing the amide bond from readily accessible reagents.

Design, synthesis and inhibition activity of novel cyclic peptides against protein tyrosine phosphatase A from Mycobacterium tuberculosis

Mycobacterium tuberculosis, the causative agent for tuberculosis has employed several signalling molecules to sense the host cellular environment and act accordingly. For example, protein tyrosine phosphatase A (MPtpA) of M. tuberculosis, a signalling pro

Development of supramolecular organo-gel based on tripeptide skeletons

Boc-Ser-Val-Gly-OCH2Ph (31) showed high gelation abilities in the aromatic solvents, particularly in toluene. The minimum gelation concentration of 31 in toluene was 10 mg/ml, suggesting that 2500 molecules of toluene were immobilized by each m

A torsional strain mechanism to tune pitch in supramolecular helices

(Figure Presented) On the turn: Torsional strain has been used to control the pitch of helical nanostructures in the range of tens to hundreds of nanometers. In this method, sterically induced torsional strain on the primary helices forces the secondary h

Deprotection of N-Alloc amines by Pd(0)/DABCO - An efficient method for in situ peptide coupling of labile amino acids

A highly efficient one-pot deprotection/peptide coupling protocol of N-Alloc amino acids with activated N-Boc or N-Fmoc amino acids was developed in solution and on solid phase. DABCO was found to be especially effective for the deprotection of the N-Allo

Peptide derivatives specific for a Plasmodium falciparum proteinase inhibit the human erythrocyte invasion by merozoites

A specific proteinase of P. falciparum merozoites has been detected by using hydrosoluble fluorogenic peptidic substrates synthesized by classical peptide chemistry; their N-terminal end was acylated by a gluconoyl group that protects them from aminopepti