133852-23-0

Basic information

• Product Name: Fmoc-Tyr-OtBu
• Synonyms: Fmoc-Tyr-OtBu;N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-L-tyrosine 1,1-dimethylethyl ester;(9H-Fluoren-9-yl)MethOxy]Carbonyl Tyr-OtBu
• CAS NO: 133852-23-0
• Molecular Formula: C₂₈H₂₉NO₅
• Molecular Weight: 459.53356
• Mol File: 133852-23-0.mol

Chemical Properties

• Boiling Point: 655.9±55.0 °C(Predicted)
• Appearance: /
• Density: 1.219±0.06 g/cm3(Predicted)
• Storage Temp.: 2-8°C
• PKA: 9.75±0.15(Predicted)
• CAS DataBase Reference: Fmoc-Tyr-OtBu(CAS DataBase Reference)
• NIST Chemistry Reference: Fmoc-Tyr-OtBu(133852-23-0)
• EPA Substance Registry System: Fmoc-Tyr-OtBu(133852-23-0)

Safety Data

• Hazardous Substances Data: 133852-23-0(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Research:
Fmoc-Tyr-OtBu is used as a building block for the synthesis of peptides and proteins. The Fmoc group provides temporary protection for the N-terminal amine of amino acids during solid-phase peptide synthesis, while the OtBu group serves as a temporary protecting group for the carboxyl group of amino acids. This allows for the controlled and stepwise assembly of peptide chains, facilitating the production of complex protein structures.
Used in Biochemistry:
Fmoc-Tyr-OtBu is used as a component in the study of protein structure and function. The tyrosine residue, an aromatic amino acid, plays a significant role in the overall structure and function of proteins. By incorporating Fmoc-Tyr-OtBu into peptide and protein synthesis, researchers can investigate the effects of tyrosine on protein folding, stability, and interactions with other biomolecules.
Used in Drug Development:
Fmoc-Tyr-OtBu is used as a precursor in the development of therapeutic peptides and proteins. The ability to synthesize specific peptide sequences with controlled protection groups allows for the design and optimization of bioactive molecules with potential applications in treating various diseases and conditions.
Used in Diagnostics:
Fmoc-Tyr-OtBu can be used as a component in the development of diagnostic tools, such as immunoassays or biosensors, that rely on the specific recognition and binding of peptides or proteins. The incorporation of Fmoc-Tyr-OtBu into these diagnostic systems can enhance their sensitivity, specificity, and overall performance.

Upstream product

• 16874-12-7 Tyr(tBu) 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 98946-18-0 tert-Butyl 2,2,2-trichloroacetimidate 
• 112883-29-1 N-Fmoc-Tyr-OH 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 60-18-4 L-tyrosine 
• 75-65-0 tert-butyl alcohol 

Downstream Products

• 944560-15-0 3-(4-{(2-cyano-ethoxy)-[1-(2-nitro-phenyl)-ethoxy]-phosphanyloxy}-phenyl)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-propionic acid tert-butyl ester 
• 600173-03-3 N-α-Fmoc-phospho(1-nitrophenylethyl-2-cyanoethyl)-L-tyrosine tert-butyl ester 
• 1159059-96-7 C₄₀H₃₇NO₅ 
• 1159059-91-2 C₃₅H₃₅NO₆ 
• 1159059-93-4 C₃₇H₃₀F₉NO₅ 
• 1159059-69-4 C₃₄H₃₃NO₅ 
• 1151854-03-3 tert-butyl Nα-[(fluoren-9-yl)methoxylcarbonyl]-L-tyrosine dichlorovinyl sulfate 
• 1151854-04-4 tert-butyl Nα-[(fluoren-9-yl)methoxylcarbonyl]-L-tyrosine trichloroethyl sulfate 
• 1208103-62-1 tert-butyl N-(9-fluorenylmethoxycarbonyl)-O-(4,4-bis(diethylphosphono)butyl)-L-tyrosine 
• 1261168-40-4 C₅₀H₄₄N₄O₅ 
• 1228073-12-8 Fmoc-L-Tyr(PO(OEt)2)-OtBu 
• 178432-28-5 Fmoc-L-Tyr(PO(OEt)2)-OH 

Relevant articles and documents

Orthogonal enzymatic reactions to control supramolecular hydrogelations

Enzyme-responsive hydrogels have great potential in applications of controlled drug release, tissue engineering, etc. In this study, we reported on a supramolecular hydrogel that showed responses to two enzymes, phosphatase which was used to form the hydrogels and esterase which could trigger gel-sol phase transitions. The gelation process and visco-elasticity property of the resulting gel, morphology of the nanostructures in hydrogel, and peptide conformation in the self-assembled nanostructure were characterized by rheology, transmission electron microscope (TEM), and circular dichroism (CD), respectively. Potential application of the enzyme-responsive hydrogel in drug release was also demonstrated in this study. Though only one potential application of drug release was proved in this study, the responsive hydrogel system in this study might have potentials for the applications in fields of cell culture, controlled-drug release, etc. Copyright

Efficient Building Blocks for Solid-Phase Peptide Synthesis of Spin Labeled Peptides for Electron Paramagnetic Resonance and Dynamic Nuclear Polarization Applications

Specific spin labeling allows the site-selective investigation of biomolecules by EPR and DNP enhanced NMR spectroscopy. A novel spin labeling strategy for commercially available Fmoc-amino acids is developed. In this approach, the PROXYL spin label is covalently attached to the hydroxyl side chain of three amino acids hydroxyproline (Hyp), serine (Ser) and tyrosine (Tyr) by a simple three-step synthesis route. The obtained PROXYL containing building-blocks are N-terminally protected by the Fmoc-protection group, which makes them applicable for the use in solid-phase peptide synthesis (SPPS). This approach allows the insertion of the spin label at any desired position during SPPS, which makes it more versatile than the widely used post synthetic spin labeling strategies. For the final building-blocks, the radical activity is proven by EPR. DNP enhanced solid-state NMR experiments employing these building-blocks in a TCE solution show enhancement factors of up to 26 for 1H and 13C (1H→13C cross-polarization). To proof the viability of the presented building-blocks for insertion of the spin label during SPPS the penta-peptide Acetyl-Gly-Ser(PROXYL)-Gly-Gly-Gly was synthesized employing the spin labeled Ser building-block. This peptide could successfully be isolated and the spin label activity proved by EPR and DNP NMR measurements, showing enhancement factors of 12.1±0.1 for 1H and 13.9±0.5 for 13C (direct polarization).

Synthesis and anticancer activities of proline-containing cyclic peptides and their linear analogs and congeners

A solution phase method was adopted for the synthesis of proline-containing cyclic pentapeptide 2 and total synthesis of naturally occurring cyclic heptapeptide Reniochalistatin B 3. For the synthesis of 3, both divergent and convergent strategies were used to improve the overall yield from 12 to 25%. Different N and C terminal modified linear analogs and congeners of 2 and 3 were synthesized. Both cyclic peptides 2 and 3 and their linear analogs/congeners were evaluated for anti-cancer activity against HeLa cell line, among which pentapeptide 2 h and hexapeptide 3n with N-terminal protected hexafluoroisopropyl carbamates (HFIPC) interestingly showed higher cytotoxicity with an IC50 of 2.73 and 4.3 μM, respectively compared to their Boc-protected analogs 2a (IC50 20 μM) and 3c (IC50 38.51 μM) and cyclic peptides 2 (>100 μM) and 3 (47 μM). These results were further validated by biological experiments such as colony formation and wound healing assays.

A gene vaccine carrier, preparation method and application thereof

The invention discloses a gene vaccine vector, and a preparation method and an application thereof; the gene vaccine vector is a supramolecular hydrogel formed through phosphatase catalysis of a small-molecular peptide; the small-molecular peptide has the structural formula represented by the formula (I), wherein when m=1, n=0, 1, 2 or 3; when n=1, m=1, 2 or 3. The gene vaccine vector after being loaded with DNA has the advantages of strong immunogenicity, large load capacity, no obvious toxicity and injectable immunity. The gene vaccine vector is mild in preparation conditions and simple in process.

Synthesis of BODIPY-Labeled Cholesterylated Glycopeptides by Tandem Click Chemistry for Glycocalyxification of Giant Unilamellar Vesicles (GUVs)

The glycocalyx cover membrane surfaces of all living cells. These complex architectures render their interaction mechanisms on the membrane surface difficult to study. Artificial cell-sized membranes with selected and defined glycosylation patterns may serve as a minimalistic approach to systematically study cell surface glycan interactions. The development of a facile general synthetic procedure for the synthesis of BODIPY-labeled cholesterylated glycopeptides, which can coat cell-size giant unilamellar vesicles (GUVs), is described. These peptide constructs were synthesized by: 1) solid-phase peptide synthesis (SPPS) using cholesterylated Fmoc-amino acids (Fmoc=9-fluorenylmethoxycarbonyl) followed by tandem click reactions, 2) attachment of a BODIPY-bicyclononyne (BCN) (prepared by Mitsunobu chemistry via novel aryl BCN-ethers) in the absence of a catalyst, and 3) glycosylation by means of copper(I)-catalyzed click reaction of an azidoglycan. Seven different GUV-glycoforms were prepared and four of these were evaluated with their corresponding four specific anti-glycan binding lectins.

Enzyme-controllable F-NMR turn on through disassembly of peptide-based nanospheres for enzyme detection

The enzyme tyrosinase could trigger the disassembly of peptide-based nanospheres, resulting in F-NMR signal turning on.

Self-assembled nanospheres as a novel delivery system for taxol: A molecular hydrogel with nanosphere morphology

Here we reported on the first example of a Folic acid-based molecular hydrogel with nanosphere morphology as a delivery system for Taxol.

PHOSPHONATED RIFAMYCINS AND USES THEREOF FOR THE PREVENTION AND TREATMENT OF BONE AND JOINT INFECTIONS

The present invention relates to phosphonated Rifamycins, and methods of making and using such compounds. These compounds are useful as antibiotics for prophylaxis and/or the treatment of bone and joint infections, especially for the prophylaxis and/or treatment of osteomyelitis.

Efficient solid-phase synthesis of sulfotyrosine peptides using a sulfate protecting-group strategy

(Chemical Equation Presented) Double protection: Efficient Fmoc-based solid-phase synthesis (SPPS) of sulfotyrosine (sY) peptides is achieved by incorporating the sY residue(s) as a dichlorovinyl-protected (DCV) sulfodiester(s) and using 2-methylpiperidine for Fmoc removal. After removal of the other protecting groups, the DCV group could be cleaved by mild hydrogenolysis giving the sY peptides in good yield.

Designed amino acid ATRP initiators for the synthesis of biohybrid materials

A synthetic strategy to prepare peptide-polymer conjugates with precise sites of attachment is described. Amino acids modified with atom transfer radical polymerization (ATRP) initiators for the polymerization of styrenes and hacrylates were prepared. Fmoc-4-(1-chloroethyl)-phenylalanine (5) was synthesized in four steps from Fmoc-tyrosine. HATU-mediated amidation with glycine-OMe resulted in dipeptide (6). The initiator was effective for Cu(I)/bipyridine mediated bulk polymerization of styrene. Kinetic studies indicated a controlled polymerization, with high conversion (97%), and a polydispersity index (PDI) of 1.25. Fmoc-O-(2-bromoisobutyryl)-serine tert-butyl ester (10) was synthesized from Fmoc-Ser(OTrt)-OH in three steps. This initiator was employed in the ATRP of 2-hydroxyethyl methacrylate (HEMA), and kinetic studies indicated a controlled polymerization. Different monomer to initiator ratios resulted in poly-(HEMA) of different molecular weights and narrow PDIs (1.14-1.25). Conversions were between 70 and 99%. HEMA modified with N-acetyl-D-glucosamine (GlcNAc) was also polymerized to 84% conversion and the resulting PDI was 1.19. The t-butyl ester protecting group of 10 was removed, and the resulting amino acid (11) was incorporated into VM(H)VVQTK by standard solid-phase peptide synthesis. Polymerization resulted in the glycopolymer-peptide conjugate in 93% conversion and a PDI of 1.14.