66076-54-8

Upstream product

• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 1080-06-4 L-Tyr-OMe 
• 81000-39-7 (S)-2-((tert-butoxycarbonyl)amino)-3-phenylpropanethioic S-acid 
• 60-18-4 L-tyrosine 
• 63-91-2 L-phenylalanine 
• 24424-99-5 di-tert-butyl dicarbonate 

Downstream Products

• 70930-22-2 Phe-Tyr methyl ester trifluoroacetate 
• 55288-06-7 H-Phe-Tyr-OMe 
• 5147-17-1 (3S,6S)-3-benzyl-6-(4-hydroxybenzyl)piperazine-2,5-dione 
• 66076-38-8 (S)-2-((S)-2-((tert-butoxycarbonyl)amino)-3-phenylpropanamido)-3-(4-hydroxyphenyl)propanoic acid 
• 91474-83-8 Boc-Asp(OBzl)-Arg(Mds)-Phe-Tyr-Gly-OH 
• 91474-82-7 Z-Arg(Mds)-Phe-Tyr-Gly-OBzl 
• 91474-73-6 Boc-Phe-Tyr-Gly-Met-Met-NH₂ 
• 91474-74-7 H-Phe-Tyr-Gly-Met-Met-NH₂ 
• 91474-79-2 Boc-Phe-Tyr-Gly-OBzl 
• 91474-59-8 Boc-Phe-Tyr-Gly-NHNH₂ 
• 91474-58-7 Boc-Phe-Tyr-Gly-OMe 
• 91474-80-5 H-Phe-Tyr-Gly-OBzl 
• 91474-88-3 H-Asp(OBzl)-Arg(Mds)-Phe-Tyr-Gly-Met-Met-NH₂*HCl 
• 91474-85-0 Boc-Asp(OBzl)-Arg(Mds)-Phe-Tyr-Gly-Met-Met-NH₂ 

Relevant academic research and scientific papers

Histamine H3 receptor antagonists with peptidomimetic (keto)piperazine structures to inhibit Aβ oligomerisation

Alzheime?s disease (AD) is the most prominent neurodegenerative disorder with high medical need. Protein-protein-interactions (PPI) interactions have a critical role in AD where β-amyloid structures (Aβ) build toxic oligomers. Design of disease modifying multi target directed ligand (MTDL) has been performed, which disable PPI on the one hand and on the other hand, act as procognitive antagonists at the histamine H3 receptor (H3R). The synthetized compounds are structurally based on peptidomimetic amino acid-like structures mainly as keto, diketo-, or acyl variations of a piperazine moiety connected to an H3R pharmacophore. Most of them showed low nanomolar affinities at H3R and some with promising affinity to Aβ-monomers. The structure–activity relationships (SAR) described offer new possibilities for MTDL with an optimized profile combining symptomatic and potential causal therapeutic approaches in AD.

Transition-metal ion-mediated morphological transformation of pyridine-based peptide nanostructures

Inspired by natural metallopeptides, we have rationally designed two pyridine-conjugated short peptides. These two peptide conjugates formed a pair of constitutional isomers that helped us describe their structure-function relationship. Both the isomers consisted of an equal number of aromatic amino acid residues, but shuffling was observed in the position of two key amino acids, viz; tyrosine and phenylalanine, which brought a remarkable change in their self-assembling behavior. The presence of specific functional groups and chemical diversity in both conjugates made them very active towards metal coordination. Both the constitutional isomers adopted different pathways of self-assembly, which could be further controlled or transformed by the use of transition metal ions. Interestingly, it was observed that the metal ions could precisely control the morphology of these metallopeptide nanostructures and make them more stable. Therefore, such artificial metallopeptides possess remarkable advantages over the natural counterparts primarily due to their tailor-made chemical structures.

Tyrosine-Specific Modification via a Dearomatization-Rearomatization Strategy: Access to Azobenzene Functionalized Peptides

Azobenzene functionalized peptides are of great importance in photoresponsive biosystems and photopharmacology. Herein, we report an efficient approach to prepare azobenzene functionalized peptides through late-stage modification of tyrosine-containing peptides using a dearomatization-rearomatization strategy. This approach shows good chemoselectivity and site selectivity as well as sensitive group tolerance to various peptides. This method enriches the postsynthetic modification toolbox of peptides and has great potential to be applied in medicinal chemistry and chemical biology.

Structure-Activity Relationships of cyclo(l -Tyrosyl- l -tyrosine) Derivatives Binding to Mycobacterium tuberculosis CYP121: Iodinated Analogues Promote Shift to High-Spin Adduct

A series of analogues of cyclo(l-tyrosyl-l-tyrosine), the substrate of the Mycobacterium tuberculosis enzyme CYP121, have been synthesized and analyzed by UV-vis and electron paramagnetic resonance spectroscopy and by X-ray crystallography. The introduction of iodine substituents onto cyclo(l-tyrosyl-l-tyrosine) results in sub-μM binding affinity for the CYP121 enzyme and a complete shift to the high-spin state of the heme FeIII. The introduction of halogens that are able to interact with heme groups is thus a feasible approach to the development of next-generation, tight binding inhibitors of the CYP121 enzyme, in the search for novel antitubercular compounds.

Marine natural occurring 2,5-diketopiperazines: Isolation, synthesis and optical properties

Seven 2,5-diketopiperazines (DKPs) were isolated from the Fijian marine sponge Acanthella cavernosa. NMR and circular dichroism (CD) comparison with synthetic L-L DKPs allowed us to determine unambiguously the L-L absolute configuration of the natural DKPs. This work initiated the setting up of an optical properties database of natural DKPs, including specific rotation and CD.

Synthesis, characterization and antimicrobial activity of protected dipeptides and their deprotected analogs

Peptides are the chemical compounds which consist of amino acids coupled together by peptide linkage. Peptide derivatives are synthesized by coupling the carboxyl group of one amino acid with amino group of other. Due to the possibilities of fortuitous and unintentional reactions, various protecting groups are used to protect the carboxylic acid as well as amino groups of both the amino acids. These peptide derivatives are associated with a variety of pharmacological activities including antibacterial and antifungal activities. While doing our analysis some of the dipeptides were synthesized in a reasonable yield and purity which were fully characterised by FTIR and H1 NMR. The antimicrobial activity of these derivatives was studied and these were found to be active against two strains of fungi (Aspergillus fumigatus & Pencillium chrysogenum) and two strains of bacteria (E. coli and Salmonella typhimurium). This provides for a future insight to work on the synthesis of these dipeptide derivatives to achieve their stability.

A traceless approach to amide and peptide construction from thioacids and dithiocarbamate-terminal amines

A novel and traceless strategy has been devised that allows a coupling of thioacids and dithiocarbamate-terminal amines. This strategy had been assumed to be dependent on the attachment of a functional equivalent of a cysteine side chain in earlier native chemical ligation approaches. This approach enables the traceless removal of CS2 to directly generate the desired amide bond and is compatible with a range of unprotected side chains of amino acid. The ability to produce amide or peptides by a traceless removal of the auxiliary is a significant virtue of the method. Meanwhile, the application of this new peptide-bond-forming reaction to the synthesis of novel endomorphin (EM) derivatives with various binding potencies was realized.

Smart oligopeptide gels: In situ formation and stabilization of gold and silver nanoparticles within supramolecular organogel networks

Tripeptide with redox active chemical entities based smart organogels have been used for in situ formation and stabilization of gold and silver nanoparticles within the supramolecular gel networks and the gold nanoparticles are aligned in arrays along the gel nanofibers of peptide 1-toluene gels. The Royal Society of Chemistry 2006.

Studies on Peptides. CXV. Synthesis of Hylambatin, a New Frog Skin Peptide of the Kassinin Family

Hylambatin, a dodecapeptide amide isolated from the skin of an African rhacopharid frog (Hylambates maculatus), was synthesized by two routes, by successive condensations of four fragments, i.e., (1-3), (4-5), (6-10), and (11-12) in one case and (1-3), (4