178119-93-2

Basic information

• Product Name: Fmoc-D-4-Hydroxyphenylglycine
• Synonyms: Fmoc-D-4-Hydroxyphenylglycine;(R)-2-(((9H-fluoren-9-yl)methoxy)carbonylamino)-2-(4-hydroxyphenyl)acetic acid;REF DUPL: Fmoc-D-4-Hydroxyphenylglycine;(R)-a-(Fmoc-amino)-4-hydroxybenzeneacetic acid
• CAS NO: 178119-93-2
• Molecular Formula: C₂₃H₁₉NO₅
• Molecular Weight: 389.40066
• EINECS: 1533716-785-6
• Mol File: 178119-93-2.mol

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: Fmoc-D-4-Hydroxyphenylglycine(CAS DataBase Reference)
• NIST Chemistry Reference: Fmoc-D-4-Hydroxyphenylglycine(178119-93-2)
• EPA Substance Registry System: Fmoc-D-4-Hydroxyphenylglycine(178119-93-2)

Safety Data

• Hazardous Substances Data: 178119-93-2(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
Fmoc-D-4-Hydroxyphenylglycine is used as a building block for the synthesis of peptide-based drugs. Its presence in the synthesis process allows for the creation of a wide range of bioactive peptides with specific therapeutic properties. Fmoc-D-4-Hydroxyphenylglycine's stability and solubility contribute to the efficient production of these drugs, enhancing their effectiveness in treating various medical conditions.
Used in Research and Development:
Fmoc-D-4-Hydroxyphenylglycine is utilized as a key component in the development of novel peptide-based research materials. Its unique structural properties enable the exploration of new peptide sequences and their potential applications in various scientific fields. Fmoc-D-4-Hydroxyphenylglycine's versatility in solid-phase peptide synthesis facilitates the design and synthesis of innovative peptides for research purposes.
Used in Peptide Synthesis:
Fmoc-D-4-Hydroxyphenylglycine is used as a protected amino acid in solid-phase peptide synthesis. The Fmoc protecting group ensures that the amino group remains unreactive during the synthesis process, allowing for the stepwise addition of other amino acids to form the desired peptide chain. This method streamlines the synthesis process and improves the overall yield and purity of the final product.

Upstream product

• 22818-40-2 D-4-hydroxyphenylglycine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 

Downstream Products

• 839719-66-3 pentafluorophenyl D-α-[(9H-fluoren-9-ylmethoxycarbonyl)amino]-4-hydroxybenzeneethanoate 
• 839720-47-7 (3-tert-butoxycarbonylamino-propyl)-[4-(tert-butoxycarbonyl-{3-[2-(9H-fluoren-9-ylmethoxycarbonylamino)-2-(4-hydroxy-phenyl)-acetylamino]-propyl}-amino)-butyl]-carbamic acid tert-butyl ester 
• 839720-17-1 (3-tert-butoxycarbonylamino-propyl)-[4-(tert-butoxycarbonyl-{3-[2-butyrylamino-2-(4-hydroxy-phenyl)-acetylamino]-propyl}-amino)-butyl]-carbamic acid tert-butyl ester 
• 839720-48-8 [4-({3-[2-amino-2-(4-hydroxy-phenyl)-acetylamino]-propyl}-tert-butoxycarbonyl-amino)-butyl]-(3-tert-butoxycarbonylamino-propyl)-carbamic acid tert-butyl ester 

Relevant articles and documents

Preparation method of amoxicillin

The invention provides a preparation method of amoxicillin. The amoxicillin is obtained by synthesis of amino protected raw materials, the reaction route is short, product purity is high, operation iseasy, and wide industrial application prospects are achieved.

Discovery of Nanomolar Dengue and West Nile Virus Protease Inhibitors Containing a 4-Benzyloxyphenylglycine Residue

The dengue virus (DENV) and West Nile Virus (WNV) NS2B-NS3 proteases are attractive targets for the development of dual-acting therapeutics against these arboviral pathogens. We present the synthesis and extensive biological evaluation of inhibitors that

A facile Fmoc solid phase synthesis strategy to access epimerization-prone biosynthetic intermediates of glycopeptide antibiotics

A rapid protocol based on Fmoc-chemistry for the solid phase peptide synthesis of vancomycin- and teicoplanin-type peptides is described. Epimerization of highly racemization-prone arlyglycine derivatives is suppressed through optimized Fmoc-deprotection

The effects of conformational constraints and steric bulk in the amino acid moiety of philanthotoxins on AMPAR antagonism

Philanthotoxin-343 (PhTX-343), a synthetic analogue of wasp toxin PhTX-433, is a noncompetitive antagonist at ionotropic receptors (e.g., AChR or iGluR). To determine possible effects of variations of the amino acid side chain, a library consisting of seventeen PhTX-343 analogues was prepared. Thus, tyrosine was replaced by either apolar, conformationally constrained, or bulky amino acids, whereas the acyl unit and the polyamine moiety were kept unchanged. Analogues with tertiary amide groups were prepared for the first time. Pentafluorophenyl esters were employed for amide bond formation, establishing general protocols for philanthotoxin solution- and solid-phase synthesis (39-90% and 42-54% overall yields, respectively). The analogues were tested for their ability to antagonize kainate-induced currents of 2-amino-3-(3-hydroxy-5-methyl- 4-isoxazoyl)propanoic acid receptors (AMPAR) expressed in Xenopus oocytes from rat brain mRNA. This showed that steric bulk in the amino acid moiety is well tolerated and suggests that binding to AMPAR does not involve the α-NHCO group as a donor in hydrogen bonding.