16879-80-4

Upstream product

• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 962-39-0 L-Phenylalanine benzyl ester 
• 13122-90-2 Boc-Phe-Phe-OH 
• 100-39-0 benzyl bromide 
• 1738-78-9 L-phenylalanine benzyl ester p-toluene-sulfonic acid salt 
• 4192-12-5 dicyclohexylammonium N-(tert-butoxycarbonyl)-L-phenylalaninate 
• 66617-58-1 N-(tert-butoxycarbonyl)-L-phenylalanine benzyl ester 
• 2462-32-0 L-phenylalanine benzyl ester hydrochloride 
• 63-91-2 L-phenylalanine 
• 100-51-6 benzyl alcohol 

Downstream Products

• 160940-54-5 Bn-L-Phe-L-Phe-(diketo-L-Asp)-L-Phe-L-Phe-Bn 
• 13122-90-2 Boc-Phe-Phe-OH 
• 1613392-57-6 H-Tic-Phe-Phe-OBn*TFA 
• 1632441-71-4 C₄₀H₄₃N₃O₆ 
• 70669-39-5 Phe-Phe-OBzl 
• 2667-02-9 tetraphenylalanine 
• 90297-11-3 C₅₅H₆₆N₁₂O₁₃ 
• 90297-19-1 C₆₀H₆₉N₁₁O₁₂ 
• 90297-06-6 C₅₃H₆₃N₁₁O₁₂ 

Relevant academic research and scientific papers

Modifying ICCA with trp-phe-phe to enhance in vivo activity and form nano-medicine

Background: 1-(4-isopropylphenyl)-β-carboline-3-carboxylic acid (ICCA) was modified by Trp-Phe-Phe to form 1-(4-isopropylphenyl)-β-carboline-3-carbonyl-Trp-Phe-Phe (ICCA-WFF). Purpose: The object of preparing ICCA-WFF was to enhance the in vivo efficacy of ICCA, to explore the possible targeting action, and to visualize the nano-feature. Methods: The advantages of ICCA-WFF over ICCA were demonstrated by a series of in vivo assays, such as anti-tumor assay, anti-arterial thrombosis assay, anti-venous thrombosis assay, P-selectin expression assay, and GPIIb/IIIa expression assay. The nano-features of ICCA-WFF were visualized by TEM, SEM and AFM images. The thrombus targeting and tumor-targeting actions were evidenced by FT-MS spectrum analysis. Results: The minimal effective dose of ICCA-WFF slowing tumor growth and inhibiting thrombosis was 10-fold lower than that of ICCA. ICCA-WFF, but not ICCA, formed nano-particles capable of safe delivery in blood circulation. In vivo ICCA-WFF, but not ICCA, can target thrombus and tumor. In thrombus and tumor, ICCA-WFF released Trp-Phe-Phe and/or ICCA. Conclusion: Modifying ICCA with Trp-Phe-Phe successfully enhanced the anti-tumor activity, improved the anti-thrombotic action, formed nano-particles, targeted tumor tissue and thrombus, and provided an oligopeptide modification strategy for heterocyclic compounds.

Self-Assembly of Tetraphenylalanine Peptides

Three different tetraphenylalanine (FFFF) based peptides that differ at the N- and C-termini have been synthesized by using standard procedures to study their ability to form different nanoassemblies under a variety of conditions. The FFFF peptide assembles into nanotubes that show more structural imperfections at the surface than those formed by the diphenylalanine (FF) peptide under the same conditions. Periodic DFT calculations (M06L functional) were used to propose a model that consists of three FFFF molecules defining a ring through head-to-tail NH3+?-OOC interactions, which in turn stack to produce deformed channels with internal diameters between 12 and 16 ?. Depending on the experimental conditions used for the peptide incubation, N-fluorenylmethoxycarbonyl (Fmoc) protected FFFF self-assembles into a variety of polymorphs: ultra-thin nanoplates, fibrils, and star-like submicrometric aggregates. DFT calculations indicate that Fmoc-FFFF prefers a parallel rather than an antiparallel β-sheet assembly. Finally, coexisting multiple assemblies (up to three) were observed for Fmoc-FFFF-OBzl (OBzl = benzyl ester), which incorporates aromatic protecting groups at the two peptide terminals. This unusual and noticeable feature is attributed to the fact that the assemblies obtained by combining the Fmoc and OBzl groups contained in the peptide are isoenergetic. Variety show! Three different tetraphenylalanine-based peptides that differ at the N- and C-termini have been synthesized by using standard procedures to study their ability to form different nanoassemblies (e.g., nanotubes, see figure) under a variety of conditions.

Effect of Solvent Choice on the Self-Assembly Properties of a Diphenylalanine Amphiphile Stabilized by an Ion Pair

A diphenylalanine (FF) amphiphile blocked at the C terminus with a benzyl ester (OBzl) and stabilized at the N terminus with a trifluoroacetate (TFA) anion was synthetized and characterized. Aggregation of peptide molecules was studied by considering a pe

Structures of L-Phenylalanine Dimers, N-(tert-Butoxycarbonyl)-L-phenylalanyl-L-phenylalanine Benzyl Ester (Boc-Phe-Phe-OBzl) and L-Phenylalanyl-L-phenylalanine Ethyl Ester Trifluoroacetate (Phe-Phe-OEt*Tfa)

The crystal structures of the title compounds have been determined by the direct method and refined by the block-diagonal least-squares method.Boc-Phe-Phe-OBzl has space group P21, with a = 14.363 (3), b = 19.016 (5), c = 5.077 (1) Angstroem, β = 97.02 (2) deg, V = 1376.3 (8) Angstroem3, Z = 2, and R = 0.070 for 1921 reflections; Phe-Phe-OEt*Tfa has space group P212121, with a = 16.507 (4), b = 24.927 (7), c = 5.650 (1) Angstroem, V = 2325 (1) Angstroem3, Z = 4, and R = 0.074 for 1544 reflections.The former crystallizes in the parallel β pleated sheet.Deviation of the main-chain conformation from that of the typical β sheet due to the substitution of bulky terminal groups is observed.The latter molecule is not in the β sheet, but has a column structure with a hydrophilic core of hydrogen bonds and a hydrophobic shell.

METHOD FOR PRODUCING CARBOXYLIC ACID AMIDE COMPOUND, AND CATALYST AND FLOW PRODUCTION SYSTEM

PROBLEM TO BE SOLVED: To provide a new production method that allows a dehydration condensation reaction between carboxylic acid and amine, and a catalyst. SOLUTION: A method for producing a carboxylic acid amide compound includes the step for causing a r

Catalytic dehydrative peptide synthesis with gem-diboronic acids

Alkane-gem-diboronic acids have emerged as versatile organoboron catalysts for dehydrative amidation of α-Amino acids. A phenol-substituted multiboron catalyst with a B-C-B structure outperformed simple arylboronic acids in the condensation of α-Amino acids with suppressed epimerization of electrophiles. gem-diboronic acid catalysis were compatible with various O, N, and S-functionalized α-Amino acids bearing N-protecting groups including common carbamates used in peptide synthesis (Boc, Cbz, Fmoc). N-Trifluoroacetyl protection enabled an unprecedented catalytic dehydrative peptide synthesis at room temperature. Preliminary mechanistic studies revealed carboxylate-binding nature of gem-diboronic acids, orthogonal to the activation of carboxylic acids by arylboronic acids. The distinctive reactivity of the gem-diboronic acids would open prospects for mild catalytic peptide condensation.

Design, synthesis, and evaluation of cystargolide-based β-lactones as potent proteasome inhibitors

The peptidic β-lactone proteasome inhibitors (PIs) cystargolides A and B were used to conduct structure-activity relationship (SAR) studies in order to assess their anticancer potential. A total of 24 different analogs were designed, synthesized and evaluated for proteasome inhibition, for cytotoxicity towards several cancer cell lines, and for their ability to enter intact cells. X-ray crystallographic analysis and subunit selectivity was used to determine the specific subunit binding associated with the structural modification of the β-lactone (P1), peptidic core, (Px and Py), and end-cap (Pz) of our scaffold. The cystargolide derivative 5k, structurally unique at both Py and P1, exhibited the most promising inhibitory activity for the β5 subunit of human proteasomes (IC50 = 3.1 nM) and significant cytotoxicity towards MCF-7 (IC50 = 416 nM), MDA-MB-231 (IC50 = 74 nM) and RPMI 8226 (IC50 = 41 nM) cancer cell lines. Cellular infiltration assays revealed that minor structural modifications have significant effects on the ability of our PIs to inhibit intracellular proteasomes, and we identified 5k as a promising candidate for continued therapeutic studies. Our novel drug lead 5k is a more potent proteasome inhibitor than carfilzomib with mid-to-low nanomolar IC50 measurements and it is cytotoxic against multiple cancer cell lines at levels approaching those of carfilzomib.

Photocyclization of Tetra- and Pentapeptides Containing Adamantylphthalimide and Phenylalanines: Reaction Efficiency and Diastereoselectivity

A series of tetrapeptides and pentapeptides was synthesized bearing a phthalimide chromophore at the N-terminus. The C-terminus of the peptides was strategically substituted with an amino acid, Phe, Phe(OMe), or Phe(OMe)2 characterized by different oxidation potentials. The photochemical reactivity of the peptides was investigated by preparative irradiation and isolation of photoproducts, as well as with laser flash photolysis. Upon photoexcitation, the peptides undergo photoinduced electron transfer (PET) and decarboxylation, followed by diastereoselective cyclization with the retention of configuration for tetrapeptides or inversion of configuration for pentapeptides. Molecular dynamics (MD) simulations and NOE experiments enabled assignment of the stereochemistry of the cyclic peptides. MD simulations of the linear peptides disclosed conformational reasons for the observed diastereoselectivity, being due to the peptide backbone spatial orientation imposed by the Phe amino acids. The photochemical efficiency for the decarboxylation and cyclization is not dependent on the peptide length, but it depends on the oxidation potential of the amino acid at the C-terminus. The results described herein are particularly important for the rational design of efficient photochemical reactions for the preparation of cyclic peptides with the desired selectivity.

One-pot isomerization-cross metathesis-reduction (ICMR) synthesis of lipophilic tetrapeptides

An efficient, versatile and rapid method toward homologue series of lipophilic tetrapeptide derivatives (herein, the opioid peptides H-TIPP-OH and H-DIPP-OH) is reported. High atom economy and a minimal number of synthetic steps resulted from a one-pot ta

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