1301706-86-4

Basic information

• Product Name: FMOC-D-THR(ME)-OH
• Synonyms: FMOC-D-THR(ME)-OH;FMOC-O-METHYL-D-THREONINE;N-alpha-(9-Fluorenylmethyloxycarbonyl)-O-methyl-D-threonine;Fmoc-O-methyl-D-threonine≥ 99% (HPLC)
• CAS NO: 1301706-86-4
• Molecular Formula: C20H21NO5
• Molecular Weight: 355.38
• Product Categories: Fluorenes, Flurenones
• Mol File: 1301706-86-4.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• Storage Temp.: Store at 0°C
• CAS DataBase Reference: FMOC-D-THR(ME)-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-D-THR(ME)-OH(1301706-86-4)
• EPA Substance Registry System: FMOC-D-THR(ME)-OH(1301706-86-4)

Safety Data

• Hazardous Substances Data: 1301706-86-4(Hazardous Substances Data)

Usage

Description

FMOC-D-THR(ME)-OH is a chemical compound that belongs to the category of FMOC (9-fluorenylmethoxycarbonyl) protected amino acids. Its chemical structure consists of FMOC as the protecting group, D-THR as the amino acid, and ME as the methyl group. FMOC-D-THR(ME)-OH is a crucial component in the field of peptide synthesis, offering a versatile and efficient approach to the construction of peptides and proteins.

Uses

Used in Pharmaceutical Industry:
FMOC-D-THR(ME)-OH is used as a building block for the synthesis of peptides and proteins, playing a vital role in the development of new drugs and therapeutic agents. Its incorporation into peptide structures allows for the exploration of novel bioactive compounds with potential applications in treating various diseases and medical conditions.
Used in Biochemistry Research:
FMOC-D-THR(ME)-OH serves as a fundamental component in the study of peptide and protein structure, function, and interactions. Researchers utilize this compound to investigate the properties of peptides and proteins, contributing to a deeper understanding of biological processes and the development of new diagnostic and therapeutic tools.
Used in Biotechnology Applications:
FMOC-D-THR(ME)-OH is employed as a starting material for the solid-phase synthesis of peptides, a technique widely used in biotechnology. The FMOC protecting group can be easily removed under mild conditions, enabling the exposure of the amino group for further coupling reactions. This feature makes FMOC-D-THR(ME)-OH an essential tool in the design and production of bioactive peptides and proteins for various biotechnological applications, such as enzyme catalysis, drug delivery, and vaccine development.

Upstream product

• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 48068-25-3 (2S,3R)-2-((tert-butoxycarbonyl)amino)-3-methoxybutanoic acid 
• 4144-02-9 O-methyl-L-threonine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 

Relevant articles and documents

General Fmoc-Based Solid-Phase Synthesis of Complex Depsipeptides Circumventing Problematic Fmoc Removal

Development of an Fmoc-based solid-phase depsipeptide methodology has been hampered by base-promoted fragmentation and diketoperazine formation upon Fmoc group elimination. Such a strategy would be a useful tool given the number of commercially available Fmoc-protected residues. Herein we report that the addition of small percentages of organic acids to the Fmoc-removal cocktail proves effective to circumvent these drawbacks and most importantly, allowed the development of an exclusively solid-phase stepwise methodology to prepare a highly complex depsipeptide with multiple and consecutive esters bonds. Alongside, the optimal protecting group scheme for residue incorporation, which is not as straightforward as it is for traditional peptide synthesis, was explored. The developed stepwise strategy proved effective for the synthesis of a highly complex cyclodepsipeptide, being comparable to the yields obtained when using traditional combined chemistry approaches.

Combinatorial Solid-Phase Synthesis and Biological Evaluation of Cyclodepsipeptide Destruxin B as a Negative Regulator for Osteoclast Morphology

Combinatorial synthesis and biological evaluation of cyclodepsipeptide destruxin B have been achieved. The cyclization precursors were prepared by solid-phase peptide synthesis via a split and pool method utilizing SynPhase lanterns with colored tags and cogs, followed by cleavage from the polymer-support. Macrolactonization utilizing MNBA-DMAPO in solution-phase was successfully performed in parallel to afford the desired 64-member destruxin analogues in moderate to good yields. Biological evaluation of the synthesized analogues indicated that a MeAla residue for the building block A is required to induce the desired morphological changes in osteoclast-like multinuclear cells (OCLs), and introduction of the substituent at the R4 position of a proline moiety is tolerated by the morphology and may enable the preparation of a molecular probe for the target identification in the osteoclasts.