138797-71-4

Basic information

• Product Name: Fmoc-O-tert-butyl-D-threonine
• Synonyms: FMOC-O-TERT-BUTYL-D-THREONINE;FMOC-O-T-BUTYL-D-THREONINE;FMOC-D-THREONINE(O-T-BUTYL);FMOC-D-THR(TBU)-OH;FMOC-D-THR(BUT);FMOC-D-THR(BUT)-OH;FMOC-D-THREONINE(TBU)-OH;9-FLUORENYLMETHOXYCARBONYL-O-T-BUTYL-D-THREONINE
• CAS NO: 138797-71-4
• Molecular Formula: C23H27NO5
• Molecular Weight: 397.46
• Product Categories: Amino Acids;Threonine [Thr, T];Fmoc-Amino Acids and Derivatives;Fmoc-Amino acid series
• Mol File: 138797-71-4.mol

Chemical Properties

• Melting Point: ~130 °C
• Boiling Point: 581.7 °C at 760 mmHg
• Flash Point: 305.6 °C
• Appearance: Pale yellow/Powder
• Density: 1.197 g/cm³
• Vapor Pressure: 2.24E-14mmHg at 25°C
• Refractive Index: 1.568
• Storage Temp.: 2-8°C
• Solubility: soluble in Methanol
• PKA: 3.42±0.10(Predicted)
• BRN: 8796152
• CAS DataBase Reference: Fmoc-O-tert-butyl-D-threonine(CAS DataBase Reference)
• NIST Chemistry Reference: Fmoc-O-tert-butyl-D-threonine(138797-71-4)
• EPA Substance Registry System: Fmoc-O-tert-butyl-D-threonine(138797-71-4)

Safety Data

• WGK Germany: 3
• F: 10
• Hazardous Substances Data: 138797-71-4(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
Fmoc-O-tert-butyl-D-threonine is used as a building block for the synthesis of complex peptides and glycopeptides, particularly those with central nervous system (CNS) activity. Its application is significant in the development of opioid glycopeptides, which are potential drug candidates capable of penetrating the blood-brain barrier to produce potent central effects.
Used in Biochemical Research:
In the field of biochemistry, Fmoc-O-tert-butyl-D-threonine is utilized as a reagent for the study and manipulation of peptide structures. Its unique properties allow researchers to investigate the interactions and functions of peptides in biological systems, contributing to a better understanding of their roles in various biological processes.
Used in Drug Development:
Fmoc-O-tert-butyl-D-threonine is also employed in the development of novel therapeutic agents targeting the central nervous system. Its incorporation into peptide and glycopeptide structures enables the creation of compounds with enhanced bioavailability and the ability to cross the blood-brain barrier, making it a valuable tool in the search for effective treatments for neurological disorders and other CNS-related conditions.

InChI:InChI=1/C23H27NO5/c1-14(29-23(2,3)4)20(21(25)26)24-22(27)28-13-19-17-11-7-5-9-15(17)16-10-6-8-12-18(16)19/h5-12,14,19-20H,13H2,1-4H3,(H,24,27)(H,25,26)/t14-,20+/m0/s1

Upstream product

• 4378-13-6 (O-tert-butyl)-L-threonine 
• 102774-86-7 9-fluorenylmethyl N-succinimidyl carbonate 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 132776-34-2 O-tert-Butyl-L-threonine Methyl Ester p-Toluenesulfonate 
• 275827-11-7 N-(9-Fluorenylmethoxycarbonyl)-O-(tert-butyl)-L-threonin-(2-phenyl-2-trimethylsilyl)ethylester 
• 73731-37-0 Fmoc-Thr-OH 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 1254943-38-8 C₈H₁₇NO₃*ClH 
• 67-56-1 methanol 
• 72-19-5 L-threonine 
• 115-11-7 isobutene 
• 119323-52-3 (2R,3R)-2-Amino-3-tert-butoxy-butyric acid 
• 130674-54-3 (2R,3R)-2-N-(9-fluorenylmethyloxycarbonyl)-D-allothreonine 
• 201353-89-1 O-tert-butyl-L-allo-threonine 

Downstream Products

• 120792-09-8 O-tert-Butyl-N-(9-fluorenylmethoxycarbonyl)-L-threonyl-N^ε-(tert-butoxycarbonyl)-L-lysyl-N^ε-(tert-butoxycarbonyl)-L-lysyl-O-tert-butyl-L-threonin-benzylester 

Relevant articles and documents

Fungal Dioxygenase AsqJ Is Promiscuous and Bimodal: Substrate-Directed Formation of Quinolones versus Quinazolinones

Previous studies showed that the FeII/α-ketoglutarate dependent dioxygenase AsqJ induces a skeletal rearrangement in viridicatin biosynthesis in Aspergillus nidulans, generating a quinolone scaffold from benzo[1,4]diazepine-2,5-dione substrates. We report that AsqJ catalyzes an additional, entirely different reaction, simply by a change in substituent in the benzodiazepinedione substrate. This new mechanism is established by substrate screening, application of functional probes, and computational analysis. AsqJ excises H2CO from the heterocyclic ring structure of suitable benzo[1,4]diazepine-2,5-dione substrates to generate quinazolinones. This novel AsqJ catalysis pathway is governed by a single substituent within the complex substrate. This unique substrate-directed reactivity of AsqJ enables the targeted biocatalytic generation of either quinolones or quinazolinones, two alkaloid frameworks of exceptional biomedical relevance.

Unwanted hydrolysis or α/β-peptide bond formation: How long should the rate-limiting coupling step take?

Nowadays, in Solid Phase Peptide Synthesis (SPPS), being either manual, automated, continuous flow or microwave-assisted, the reaction with various coupling reagents takes place via in situ active ester formation. In this study, the formation and stability of these key active esters were investigated with time-resolved 1H NMR by using the common PyBOP/DIEA and HOBt/DIC coupling reagents for both α- and β-amino acids. Parallel to the amide bond formation, the hydrolysis of the α/β-active esters, a side reaction that is a considerable efficacy limiting factor, was studied. Based on the chemical nature/constitution of the active esters, three amino acid categories were determined: (i) the rapidly hydrolyzing ones (t 24 h) in solution. The current insight into the kinetics of this key hydrolysis side reaction serves as a guide to optimize the coupling conditions of α- and β-amino acids, thereby saving time and minimizing the amounts of reagents and amino acids to be used-all key factors of more environmentally friendly chemistry.

Asymmetric synthesis of (2S,3S)-3-Me-glutamine and (R)-allo-threonine derivatives proper for solid-phase peptide coupling

Practical new routes for preparation of (2S,3S)-3-Me-glutamine and (R)-allo-threonine derivatives, the key structural components of cytotoxic marine peptides callipeltin O and Q, suitable for the Fmoc-SPPS, were developed. (2S,3S)-Fmoc-3-Me-Gln(Xan)-OH was synthesized via Michael addition reactions of Ni (II) complex of chiral Gly-Schiff base; while Fmoc-(R)-allo-Thr-OH was prepared using chiral Ni (II) complex-assisted α-epimerization methodology, starting form (S)-Thr(tBu)-OH.

A Fmoc - Thr (tBu) - OH preparation method (by machine translation)

The invention discloses a Fmoc - Thr (tBu) - OH of the preparation method, relates to the field of chemical technology. The method comprises: methanol, thionyl chloride, Thr are mixed, the reaction produces Thr?OMe?HCl solution; to the Thr?OMe?HCl solution enters dichloromethane, and inject the isobutene, at the same time add sulfuric acid to maintain the acidic environment, reaction (tBu) Thr??OMe solution; will be Thr??OMe solution (tBu) saponification by alkali Thr?(tBu), then add Fmoc - OSu reaction to obtain the elementary product Fmoc - Thr (tBu) - OH; the taste for the Fmoc - Thr (tBu) - OH to obtain the Fmoc - Thr (tBu) - OH product. The method can effectively shorten the production steps, can improve the production efficiency and yield, is suitable for modern industrial production. (by machine translation)

Improved synthesis of d-allothreonine derivatives from l-threonine

The improved synthesis of protected d-allothreonine derivatives [Fmoc-d-alloThr(tBu)-OH (1) and Fmoc-d-alloThr-OtBu (2)] is described. The epimerization of cheap l-threonine (l-Thr) (3) with catalytic salicylaldehyde afforded a mixture of l-Thr (3) and d-alloThr (4) and separation of ammonium salt gave d-alloThr (4) in 96% de. The chemoselective deprotection of tert-butyl ether or tert-butyl ester of Fmoc-d-alloThr(tBu)-O tBu (5) easily succeeded in converting Fmoc-d-alloThr( tBu)-OH (1) or Fmoc-d-alloThr-OtBu (2), respectively.

A one-pot procedure for the preparation of N-9-fluorenylmethyloxycarbonyl- α-amino diazoketones from α-amino acids

The study describes a new "one-pot" route to the synthesis of N-9-fluorenylmethyloxycarbonyl (Fmoc) α-amino diazoketones. The procedure was tested on a series of commercially available free or side-chain protected α-amino acids employed as precursors. The conversion into the title compounds was achieved by masking and activating the α-amino acids with a single reagent, namely, 9-fluorenylmethyl chloroformate (Fmoc-Cl). The resulting N-protected mixed anhydrides were reacted with diazomethane to lead to the α-amino diazoketones, which were isolated by flash column chromatography in very good to excellent overall yields. The versatility of the procedure was verified on lipophilic α-amino acids and further demonstrated by the preparation of N-Fmoc-α-amino diazoketones also from α-amino acids containing side-chain masking groups, which are orthogonal to the Fmoc one. The results confirmed that tert-butyloxycarbonyl (Boc), tert-butyl (tBu), and 2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl (Pbf), three acid-labile protecting groups mostly adopted in the solution and solid-phase peptide synthesis, are compatible to the adopted reaction conditions. In all cases, the formation of the corresponding C-methyl ester of the starting amino acid was not observed. Moreover, the proposed method respects the chirality of the starting α-amino acids. No racemization occurred when the procedure was applied to the synthesis of the respective N-Fmoc-protected α-amino diazoketones from l-isoleucine and l-threonine and to the preparation of a diastereomeric pair of N-Fmoc-protected dipeptidyl diazoketones.

Derivates of Polyethylene Glycol Modified Thymosin Alpha 1

Pharmaceutical compositions that include thymosin alpha 1 peptide derivatives modified at the C-terminal of the peptide chain with polyethylene glycol, and their pharmaceutical acceptable salts, are generally disclosed. Also, new methods used to prepare these thymosin alpha 1 peptide derivatives modified at the C-terminal of the peptide chain with polyethylene glycol are generally provided. The presently disclosed compounds and their salts can be prepared administered to humans to treat immune disease and can also be used in adjuvant treatment.

Total synthesis of the large non-ribosomal peptide polytheonamide B

Polytheonamide B is by far the largest non-ribosomal peptide known at present, and displays extraordinary cytotoxicity (EC50 =68 pg ml -1 , mouse leukaemia P388 cells). Its 48 amino-acid residues include a variety of non-proteinogenic d- and l-amino acids, and the absolute stereochemistry of these amino acids alternate in sequence. These structural features induce the formation of a stable β-strand-type structure, giving rise to an overall tubular structure over 30A? in length. In a biological setting, this fold is believed to transport cations across the lipid bilayer through a pore, thereby acting as an ion channel. Here, we report the first chemical construction of polytheonamide B. Our synthesis relies on the combination of four key stages: syntheses of non-proteinogenic amino acids, a solid-phase assembly of four fragments of polytheonamide B, silver-mediated connection of the fragments and, finally, global deprotection. The synthetic material now available will allow studies of the relationships between its conformational properties, channel functions and cytotoxicity.

GLP-2 compounds, formulations, and uses thereof

The present invention relates to novel human glucagon-like peptide-2 (GLP-2) peptides and human glucagon-like peptide-2 derivatives which have a protracted profile of action as well as polynucleotide constructs encoding such peptides, vectors and host cells comprising and expressing the polynucleotide, pharmaceutical compositions, uses and methods of treatment.

(2-Phenyl-2-trimethylsilyl)ethyl (PTMSE) esters - A novel carboxyl protecting group

A novel silicon-containing protecting group based on the known 2- (trimethylsilyl)ethyl system has been developed for the protection of the carboxylic group, e.g. in peptide chemistry. The new protecting group can be cleaved by treatment with tetra-n-butylammonium fluoride much more rapidly than the known 2-(trimethylsilyl)ethyl group, leading to less side reactions.