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
• Article Data: 13

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

General Description

Fmoc-Tyr-OtBu is a chemical compound that consists of an N-terminal protecting group (Fmoc), a tyrosine residue, and a C-terminal protecting group (OtBu). The Fmoc group is commonly used in solid-phase peptide synthesis as a temporary protection for the N-terminal amine of amino acids. The tyrosine residue is an aromatic amino acid that plays a crucial role in protein structure and function. The OtBu group is an alkyl group used as a temporary protecting group for the carboxyl group of amino acids during peptide synthesis. Overall, Fmoc-Tyr-OtBu is a key component in the synthesis of peptides and proteins, and its precise structure and functionality make it important in the field of biochemistry and pharmaceutical research.

Upstream product

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

Downstream Products

• 1159059-96-7 C₄₀H₃₇NO₅ 
• 1159059-91-2 C₃₅H₃₅NO₆ 
• 1159059-93-4 C₃₇H₃₀F₉NO₅ 
• 1159059-69-4 C₃₄H₃₃NO₅ 
• 1151854-04-4 tert-butyl Nα-[(fluoren-9-yl)methoxylcarbonyl]-L-tyrosine trichloroethyl sulfate 
• 16874-12-7 Tyr(tBu) 
• 71989-38-3 Fmoc-Tyr(tBu)-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 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.