110797-35-8

Basic information

• Product Name: NALPHA-FMOC-L-SERINE TERT-BUTYL ESTER
• Synonyms: N-ALPHA-(9-FLUORENYLMETHOXYCARBONYL)-L-SERINE ALPHA-T-BUTYL ESTER;NALPHA-[(9H-FLUOREN-9-YLMETHOXY)CARBONYL]-L-SERINE TERT-BUTYL ESTER;NALPHA-FMOC-L-SERINE TERT-BUTYL ESTER;FMOC-SER-OTBU;Nα-Fmoc-L-serine tert-Butyl Ester;Nalpha-Fmoc-L-serine tert-Butyl Ester Fmoc-Ser-OtBu;Nα-[(9H-Fluoren-9-ylMethoxy)carbonyl]-L-serine tert-Butyl Ester;-[(9H-Fluoren-9-ylmethoxy)carbonyl]-L-serine tert-Butyl Ester
• CAS NO: 110797-35-8
• Molecular Formula: C₂₂H₂₅NO₅
• Molecular Weight: 383.44
• Product Categories: Amino Acid tert-Butyl Esters;Amino Acids;Amino Acids (C-Protected);Amino Acids (N-Protected);Biochemistry;Fmoc-Amino Acids;Reagents for Oligosaccharide Synthesis
• Mol File: 110797-35-8.mol

Chemical Properties

• Melting Point: 127 °C
• Boiling Point: 588.356oC at 760 mmHg
• Flash Point: 309.627oC
• Appearance: /
• Density: 1.217g/cm3
• Vapor Pressure: 0mmHg at 25°C
• Refractive Index: 11 ° (C=1, CHCl3)
• Storage Temp.: Refrigerator
• Solubility: soluble in Chloroform
• PKA: 10.07±0.46(Predicted)
• CAS DataBase Reference: NALPHA-FMOC-L-SERINE TERT-BUTYL ESTER(CAS DataBase Reference)
• NIST Chemistry Reference: NALPHA-FMOC-L-SERINE TERT-BUTYL ESTER(110797-35-8)
• EPA Substance Registry System: NALPHA-FMOC-L-SERINE TERT-BUTYL ESTER(110797-35-8)

Safety Data

• Hazardous Substances Data: 110797-35-8(Hazardous Substances Data)

Usage

Uses

Used in Organic Chemistry Research:
NALPHA-FMOC-L-SERINE TERT-BUTYL ESTER is used as a synthetic building block for the preparation of complex organic molecules, leveraging its protective groups to control the reactivity and selectivity of chemical reactions.
Used in Biochemistry Research:
NALPHA-FMOC-L-SERINE TERT-BUTYL ESTER is used as a component in the synthesis of peptide and protein derivatives, allowing researchers to explore the structure, function, and interactions of these biomolecules in various biological systems.
Used in Pharmaceutical Development:
NALPHA-FMOC-L-SERINE TERT-BUTYL ESTER is used as a key intermediate in the development of novel drugs and therapeutic agents, taking advantage of its versatility in peptide synthesis to create potential candidates with specific biological activities.
Used in Peptide Synthesis:
NALPHA-FMOC-L-SERINE TERT-BUTYL ESTER is used as a protected amino acid in solid-phase peptide synthesis, providing a reliable method to construct peptide sequences with controlled coupling and deprotection steps.
Used in Protein Engineering:
NALPHA-FMOC-L-SERINE TERT-BUTYL ESTER is used as a modular unit in protein engineering, enabling the incorporation of non-natural amino acids or post-translational modifications into proteins to study their effects on protein function and stability.
Used in Chemical Biology:
NALPHA-FMOC-L-SERINE TERT-BUTYL ESTER is used as a tool in chemical biology to investigate the interactions between small molecules and biomacromolecules, contributing to the understanding of molecular recognition and signaling processes.

InChI:InChI=1/C22H25NO5/c1-22(2,3)28-20(25)19(12-24)23-21(26)27-13-18-16-10-6-4-8-14(16)15-9-5-7-11-17(15)18/h4-11,18-19,24H,12-13H2,1-3H3,(H,23,26)/t19-/m0/s1

Upstream product

• 98946-18-0 tert-Butyl 2,2,2-trichloroacetimidate 
• 73724-45-5 N-(9H-fluoren-9-ylmethoxycarbonyl)-L-serine 
• 75-65-0 tert-butyl alcohol 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 111061-56-4 Fmoc-Ser(Trt)-OH 
• 59859-77-7 2-benzyloxycarbonylamino-3-hydroxy-propionic acid tert-butyl ester 
• 90048-49-0 tert-butyl (2S)-2-amino-3-hydroxypropanoate 
• 120791-74-4 O-(Acetoacetyl)-N-(9-fluorenylmethoxycarbonyl)-L-serin 
• 122889-11-6 O-benzyl-N-Fmoc-L-serine 
• 305836-50-4 (S)-3-benzyloxy-2-(9H-fluoren-9-ylmethoxycarbonylamino)propionic acid tert-butyl ester 
• 600172-98-3 2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-trityloxy-propionic acid tert-butyl ester 
• 120792-31-6 O-(Acetoacetyl)-N-(9-fluorenylmethoxycarbonyl)-L-serin-tert-butylester 

Downstream Products

• 120851-33-4 N-(9-Fluorenylmethoxycarbonyl)-O-<(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1->3)-O-(2-azido-4,6-di-O-benzoyl-2-desoxy-β-D-galactopyranosyl)>-L-serin-tert-butylester 
• 120791-79-9 N-(9-Fluorenylmethoxycarbonyl)-O-<(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1->3)-O-(2-azido-4,6-di-O-benzoyl-2-desoxy-α-D-galactopyranosyl)>-L-serin-tert-butylester 
• 225663-02-5 O-(3,4,6-tri-O-benzyl-2-deoxy-2-nitro-α-D-galactopyranosyl)-N-(fluorenylmethoxycarbonyl)-L-serine tert-butyl ester 
• 600172-99-4 N-α-Fmoc-phosphi(1-nitrophenylethyl-2-cyanoethyl)-L-serine tert-butyl ester 
• 863890-86-2 (S)-3-[(2S,3R,4R,5R,6R)-3-Azido-5-benzyloxy-6-benzyloxymethyl-4-((2R,3R,4S,5S,6R)-3,4,5-tris-benzyloxy-6-benzyloxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-yloxy]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-propionic acid tert-butyl ester 
• 881995-79-5 (2R,6R)-N²,N⁶-bis(fluoren-9-ylmethoxycarbonyl)lanthionine α-tert-butyl ester 
• 881996-33-4 (2R,6S)-N²,N⁶-bis(fluoren-9-ylmethoxycarbonyl)lanthionine α-allyl ester 
• 881996-32-3 (2R,6R)-N²,N⁶-bis(fluoren-9-ylmethoxycarbonyl)lanthionine α-allyl ester 
• 886583-25-1 N-[(9-fluorenyl)methoxycarbonyl]-p-[3-(trifluoromethyl)-3H-diazirin-3-yl]-L-phenylalanine tert-butyl ester 
• 886583-24-0 N-[(9-fluorenyl)methoxycarbonyl]-p-[3-(trifluoromethyl)diaziridine]-L-phenylalanine tert-butyl ester 
• 133342-64-0 (S)-N-(9-fluorenylmethoxycarbonyl)-[4-[3-(trifluoromethyl)-3H-diazirin-3-yl]phenyl]alanine 
• 863890-94-2 (S)-3-[(2S,3R,4R,5R,6R)-3-Acetylamino-5-benzyloxy-6-benzyloxymethyl-4-((2R,3R,4S,5S,6R)-3,4,5-tris-benzyloxy-6-benzyloxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-yloxy]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-propionic acid tert-butyl ester 
• 682359-13-3 N-(9-fluorenylmethoxycarbonyl)-β-bromo-L-alanyl-L-alanine benzyl ester 
• 600173-00-0 N-α-Fmoc-phospho(1-nitrophenylethyl-2-cyanoethyl)-L-serine tert-butyl ester 

Relevant articles and documents

Synthesis of the antimicrobial S-Linked glycopeptide, glycocin F

The first total synthesis of glycocin F, a uniquely diglycosylated antimicrobial peptide bearing a rare S-linked N-acetylglucosamine (GlcNAc) moiety in addition to an O-linked GlcNAc, has been accomplished using a native chemical ligation strategy. The synthetic and naturally occurring peptides were compared by HPLC, mass spectrometry, NMR and CD spectroscopy, and their stability towards chymotrypsin digestion and antimicrobial activity were measured. This is the first comprehensive structural and functional comparison of a naturally occurring glycocin with an active synthetic analogue.

Design and synthesis of trivalent Tn glycoconjugate polymers by nitroxide-mediated polymerization

A new synthetic method for preparing Tn glycoconjugate polymers, containing tumor-associated carbohydrate antigens, by controlled living radical polymerization is reported. To mimic the authentic structures of Tn glycopeptide antigens and to explore the controlled living radical polymerization, three tumor-associated carbohydrate antigens (GalNAc, GalNAcα1-O-Ser, and GalNAcα1-O-Thr) were attached to a styrene-type monomer through a diethylene glycol spacer. Under nitroxide-mediated polymerization, controlled living radical polymerization proceeded to afford defined glycopeptide polymers with different Tn densities and compositions. The polydispersity index (PDI) and molecular weights were increased and conversions were decreased upon increasing the concentration of Tn glycoconjugate monomers. The resulting Tn glycoconjugate polymers were characterized by NMR and IR. The spectral data indicate that the Tn glycoconjugate moiety did attach to the polymer chain and Tn glycoconjugate density could be adjusted through the nitroxide-mediated polymerization conditions. The number of Tn units containing in the polymer chains could be estimated by NMR integration. This synthetic approach provides a new and efficient tool for constructing novel Tn glycoconjugate polymers.

Synthesis of selenocysteine-containing dipeptides modeling the active site of thioredoxin reductase

Four cyclic dipeptides modeling the active site of thioredoxin reductase (TrxR), UU, CU, UC, and CC, where U and C represent selenocystine and cystine, respectively, were synthesized and their glutathione peroxidase (GPx)-like catalytic activity was evaluated by the reaction of hydrogen peroxide (H2O2) with glutathione (GSH) in the presence of glutathione reductase (GR). Among these, only UC exhibited the significant antioxidant capacity, suggesting that an atomic environment around the Se–S bond is relevant to the reactivity toward a thiol substrate.

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 evaluation of peptidic thrombin inhibitors bearing acid-stable sulfotyrosine analogues

Tyrosine sulfation is an important post-translational modification of peptides and proteins which underpins and modulates many protein-protein interactions. In order to overcome the inherent instability of the native modification, we report the synthesis of two sulfonate analogues and their incorporation into two thrombin-inhibiting sulfopeptides. The effective mimicry of these sulfonate analogues for native sulfotyrosine was validated in the context of their thrombin inhibitory activity and binding mode, as determined by X-ray crystallography.

Synthesis method and application of 1-aza -5-germanium-5-alkyl bicyclic [3.3.3] undecane compound.

The invention provides a 1-aza-5-germanium hetero-5-alkyl bicyclic [3.3.3] hendecane compound having a structure shown in the formula I, and the types of the 1-aza-5-germanium hetero-5-alkyl bicyclic[3.3.3] hendecane compound are expanded. The provided compound can serve as a nucleophilic reagent, the air and humidity conditions of the nucleophilic reagent are stable, and the efficiency of the Ge-Stille coupling reaction of aryl halogen and the 1-aza-5-germanium hetero-5-alkyl bicyclic [3.3.3] hendecane compound is high.

Optimized syntheses of Fmoc azido amino acids for the preparation of azidopeptides

The rise of CuI-catalyzed click chemistry has initiated an increased demand for azido and alkyne derivatives of amino acid as precursors for the synthesis of clicked peptides. However, the use of azido and alkyne amino acids in peptide chemistry is complicated by their high cost. For this reason, we investigated the possibility of the in-house preparation of a set of five Fmoc azido amino acids: β-azido l-alanine and d-alanine, γ-azido l-homoalanine, δ-azido l-ornithine and ω-azido l-lysine. We investigated several reaction pathways described in the literature, suggested several improvements and proposed several alternative routes for the synthesis of these compounds in high purity. Here, we demonstrate that multigram quantities of these Fmoc azido amino acids can be prepared within a week or two and at user-friendly costs. We also incorporated these azido amino acids into several model tripeptides, and we observed the formation of a new elimination product of the azido moiety upon conditions of prolonged couplings with 2-(1H-benzotriazol-1-yl)-1,1,3,3-tetramethyluronium hexafluorophosphate/DIPEA. We hope that our detailed synthetic protocols will inspire some peptide chemists to prepare these Fmoc azido acids in their laboratories and will assist them in avoiding the too extensive costs of azidopeptide syntheses. Experimental procedures and/or analytical data for compounds 3–5, 20, 25, 26, 30 and 43–47 are provided in the supporting information.

Synthesis and Bioactivity of Diastereomers of the Virulence Lanthipeptide Cytolysin

Cytolysin, a two-component lanthipeptide comprising cytolysin S (CylLS″) and cytolysin L (CylLL″), is the only family member to exhibit lytic activity against mammalian cells in addition to synergistic antimicrobial activity. A subset of the thioether cross-links of CylLS″ and CylLL″ have ll stereochemistry instead of the canonical dl stereochemistry in all previously characterized lanthipeptides. The synthesis of a CylLS″ variant with dl stereochemistry is reported. Its antimicrobial activity was found to be decreased, but not its lytic activity against red blood cells. Hence, the unusual ll stereochemistry is not responsible for the lytic activity.

Chemical synthesis and biological activity of analogues of the lantibiotic epilancin 15X

Lantibiotics are a large family of antibacterial peptide natural products containing multiple post-translational modifications, including the thioether structures lanthionine and methyllanthionine. Efforts to probe structure-activity relationships and engineer improved pharmacological properties have driven the development of new methods to produce non-natural analogues of these compounds. In this study, solid-supported chemical synthesis was used to produce analogues of the potent lantibiotic epilancin 15X, in order to assess the importance of several N-terminal post-translational modifications for biological activity. Surprisingly, substitution of these moieties, including the unusual N-terminal d-lactyl moiety, resulted in relatively small changes in the antimicrobial activity and pore-forming ability of the peptides.

NITRIC OXIDE DONOR COMPOUNDS

The invention relates to nitric oxide donor compounds and their use for treatingcardiovascular diseases, inflammation, pain, fever, gastrointestinal disorders, ophthalmic diseases, hepatic disorders, renal diseases, respiratory disorders, immunological diseases, bone metabolismdysfunctions, central and peripheral nervous system diseases, sexual dysfunctions, infectious diseases, for the inhibition of platelet aggregation and platelet adhesion, for treating pathological conditions resulting from abnormal cell proliferation, vascular diseases. The invention also relates to compositions comprising at least one nitric oxide releasing compoundsof the invention and composition comprising at least one nitric oxide releasing compoundsaccording to the inventionand at least one 15 therapeutic agent.