73724-45-5

Basic information

• Product Name: Fmoc-L-Serine
• Synonyms: Fmoc-L-serine ,99%;N-FMoc-L-serine, 97+%;N-Fmoc-L-serine Fmoc-Ser-OH;L-Serine-d3-N-FMOC;FMoc-Ser-OH (FMoc-L-Serine);(S)-2-(((9H-fluoren-9-yl)Methoxy)carbonylaMino)-3-hydroxypropanoic acid;FMoc-Ser.H2O;L-SERINE-N-FMOC (13C3,15N)
• CAS NO: 73724-45-5
• Molecular Formula: C₁₈H₁₇NO₅
• Molecular Weight: 327.33
• EINECS: -0
• Product Categories: Protected Amino Acids;Amino Acids;Serine [Ser, S];Fmoc-Amino Acids and Derivatives;Amino Acids (N-Protected);Biochemistry;Fmoc-Amino Acids;Fmoc-Amino acid series
• Mol File: 73724-45-5.mol

Chemical Properties

• Melting Point: 104-106°C
• Boiling Point: 599.3 °C at 760 mmHg
• Flash Point: 316.2 °C
• Appearance: /
• Density: 1.362 g/cm³
• Vapor Pressure: 3.27E-15mmHg at 25°C
• Refractive Index: -12.5 ° (C=1, DMF)
• Storage Temp.: 2-8°C
• Solubility: soluble in Methanol
• PKA: 3.51±0.10(Predicted)
• BRN: 4715791
• CAS DataBase Reference: Fmoc-L-Serine(CAS DataBase Reference)
• NIST Chemistry Reference: Fmoc-L-Serine(73724-45-5)
• EPA Substance Registry System: Fmoc-L-Serine(73724-45-5)

Safety Data

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 22-24/25-26
• WGK Germany: 3
• Hazardous Substances Data: 73724-45-5(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
Fmoc-L-Serine is used as a building block for the synthesis of peptides and proteins due to its role as a nonessential amino acid. Its N-Fmoc protection allows for selective deprotection and coupling reactions in peptide synthesis, facilitating the production of complex peptide-based drugs and therapeutic agents.
Used in Research and Development:
Fmoc-L-Serine serves as a valuable research tool in the study of protein structure, function, and interactions. Its N-Fmoc protection enables controlled synthesis and modification of peptides and proteins, allowing researchers to investigate their properties and potential applications in various biological processes.
Used in Nutraceutical Industry:
Fmoc-L-Serine is used as a supplement in the development of nutraceutical products, given its importance in the synthesis of sphingolipids and phosphatidylserine. These compounds contribute to central nervous system neuronal survival and overall brain health, making Fmoc-L-Serine a potential ingredient in cognitive health supplements.
Used in Cosmetic Industry:
Fmoc-L-Serine can be utilized in the development of cosmetic products, particularly those targeting skin health and regeneration. Its role in the synthesis of sphingolipids, which are essential components of the skin barrier, makes it a potential ingredient in skincare formulations aimed at maintaining skin integrity and promoting healing.

InChI:InChI=1/C18H17NO5/c20-9-16(17(21)22)19-18(23)24-10-15-13-7-3-1-5-11(13)12-6-2-4-8-14(12)15/h1-8,15-16,20H,9-10H2,(H,19,23)(H,21,22)/p-1/t16-/m0/s1

Upstream product

• 312-84-5 D-Serine 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 136083-72-2 N-(9-fluorenylmethoxycarbonyl)-DL-serine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 56-45-1 L-serin 
• 88744-04-1 (9-fluorenyl)methyl pentafluorophenyl carbonate 
• 82911-71-5 Fmoc-OBT 
• 71989-33-8 Fmoc-Ser(tBu)-OH 
• 60022-62-0 L-serine benzyl ester hydrochloride 
• 82911-70-4 9-fluorenylmethyl pentachlorophenyl carbonate 
• 146346-81-8 (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-((tert-butyldimethylsilyl)oxy)propanoic acid 
• 129460-16-8 (S)-3-tert-Butoxy-2-(9H-fluoren-9-ylmethoxycarbonylamino)-propionic acid tert-butyl ester 
• 82911-78-2 N-[(9-fluorenylmethoxy)carbonyl]-L-serine methyl ester 
• 82911-74-8 Dicyclohexyl-amine; compound with benzotriazol-1-ol 

Downstream Products

• 211678-11-4 N-(9-fluorenylmethyloxycarbonyl)-O-(2,3,4,6-tetra-O-acetyl-α-D-mannopyranosyl)-D-serine 
• 874817-14-8 2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-hydroxypropionic acid methyl ester 
• 298712-42-2 N-Fmoc-D-serine tetradecylamide 

Relevant articles and documents

Tetrahydropyranyl: A Non-aromatic, Mild-Acid-Labile Group for Hydroxyl Protection in Solid-Phase Peptide Synthesis

The use of the tetrahydropyranyl (Thp) group for the protection of serine and threonine side-chain hydroxyl groups in solid-phase peptide synthesis has not been widely investigated. Ser/Thr side-chain hydroxyl protection with this acid-labile and non-aromatic moiety is presented here. Although Thp reacts with free carboxylic acids, it can be concluded that to introduce Thp ethers at the hydroxyl groups of N-protected Ser and Thr, protection of the C-terminal carboxyl group is unnecessary due to the lability of Thp esters. Thp-protected Ser/Thr-containing tripeptides are synthesized and the removal of Thp studied in low concentrations of trifluoroacetic acid in the presence of cation scavengers. Given its general stability to most non-acidic reagents, improved solubility of its conjugates and ease with which it can be removed, Thp emerges as an effective protecting group for the hydroxyl groups of Ser and Thr in solid-phase peptide synthesis.

O-SUBSTITUTED SERINE DERIVATIVE PRODUCTION METHOD

It was discovered that a cyclic sulfamidate can be produced by reacting an amino acid derivative with a cyclization reagent. In addition, it was discovered that an O-substituted serine derivative can be produced by reacting a cyclic sulfamidate with an alcohol.

Synthesis of xylose-binding cyclic octalipopeptides burkholdine-1213 analogues

The synthesis of xylose-bearing cyclic octalipopeptides burkholdine-1213 analogues is described. Sugar-containing lipopeptides are generally highly amphiphilic and often exhibit potent antifungal activities, but a synthesis of a xylose-bearing burkholdine analogue has never been reported. We prepared burkholdine-1213 analogues by solution-phase macrolactamization of xylose-bearing linear peptides obtained by incorporating the bespoke Fmoc-Ser(β-O-xyloseAc3)-OH building block into a Fmoc-solid phase peptide synthesis protocol. All analogues synthesized exhibited similar properties and moderate antifungal activities.

Scope and limitations of pseudoprolines as individual amino acids in peptide synthesis

Protected 4-carboxyoxazolidines and thiazolidines (pseudoprolines) are derivatives of serine, threonine or cysteine amino acids. Such compounds are used in peptide synthesis among the other protected amino acids. They are usually practiced when a peptide sequence is readily aggregating during synthesis due to their ability to disrupt secondary structure formation. Such compounds are usually applied as dipeptides. In present work Fmoc-protected pseudoprolines were synthesized and applied in peptide synthesis not as dipeptides but as individual amino acids. Different acylation protocols and amino acids were tested to acylate pseudoprolines. Several “difficult” peptides were synthesized to confirm the efficacy of such constructions. It was shown that pseudoprolines could be easily synthesized and used in automated or manual synthesis not as dipeptides but as ordinary amino acids.

Novel chiral stationary phases based on 3,5-dimethyl phenylcarbamoylated β-cyclodextrin combining cinchona alkaloid moiety

Novel chiral selectors based on 3,5-dimethyl phenylcarbamoylated β-cyclodextrin connecting quinine (QN) or quinidine (QD) moiety were synthesized and immobilized on silica gel. Their chromatographic performances were investigated by comparing to the 3,5-dimethyl phenylcarbamoylated β-cyclodextrin (β-CD) chiral stationary phase (CSP) and 9-O-(tert-butylcarbamoyl)-QN-based CSP (QN-AX). Fmoc-protected amino acids, chiral drug cloprostenol (which has been successfully employed in veterinary medicine), and neutral chiral analytes were evaluated on CSPs, and the results showed that the novel CSPs characterized as both enantioseparation capabilities of CD-based CSP and QN/QD-based CSPs have broader application range than β-CD-based CSP or QN/QD-based CSPs. It was found that QN/QD moieties play a dominant role in the overall enantioseparation process of Fmoc-amino acids accompanied by the synergistic effect of β-CD moiety, which lead to the different enantioseparation of β-CD-QN-based CSP and β-CD-QD-based CSP. Furthermore, new CSPs retain extraordinary enantioseparation of cyclodextrin-based CSP for some neutral analytes on normal phase and even exhibit better enantioseparation than the corresponding β-CD-based CSP for certain samples.

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.

Determination of Chemical and Enantiomeric Purity of α-Amino Acids and their Methyl Esters as N-Fluorenylmethoxycarbonyl Derivatives Using Amylose-derived Chiral Stationary Phases

Liquid chromatographic enantiomer separation and simultaneous determination of chemical and enantiomeric purity of α-amino acids and their methyl esters as N-fluorenylmethoxycarbonyl (FMOC) derivatives was performed on three covalently bonded type chiral stationary phases (CSPs) derived from amylose derivatives. The enantiomer separation of α-amino acid esters as N-FMOC derivatives was better than that of the corresponding acids, especially for CSP 1 and 2. Chemical impurities as the corresponding racemic acids present in several commercially available racemic amino acid methyl esters were observed to be 0.49–17.50%. Enantiomeric impurities of several commercially available L-amino acid methyl esters were found to be 0.03–0.58%, whereas chemical impurities as the corresponding racemic acids present in the same analytes were found to be 0.13–13.62%. This developed analytical method will be useful for the determination of chemical and enantiomeric purity of α-amino acids and/or esters as N-FMOC derivatives using amylose-derived CSPs.

Supramolecular Platform Stabilizing Growth Factors

High concentrations of supplemented growth factors can cause oversaturation and adverse effects in in vitro and in vivo studies, though these supraphysiological concentrations are often required due to the low stability of growth factors. Here we demonstrate the stabilization of TGF-β1 and BMP4 using supramolecular polymers. Inspired by heparan sulfate, sulfonated peptides were presented on a supramolecular polymer to allow for noncovalent binding to growth factors in solution. After mixing with excipient molecules, both TGF-β1 and BMP4 were shown to have a prolonged half-life compared to the growth factors free in solution. Moreover, high cellular response was measured by a luciferase assay, indicating that TGF-β1 remained highly active upon binding to the supramolecular assembly. The results demonstrate that significant lower concentrations of growth factors can be used when supramolecular polymers bearing growth factor binding moieties are implemented. This approach can also be exploited in hydrogel systems to control growth factor release.

MgI2-chemoselective cleavage for removal of amino acid protecting groups: A fresh vision for peptide synthesis

In the field of peptide synthesis, the key to a successful access to synthetic targets lies on a pertinent combination of protecting groups. Their choice is directed by their selective removal conditions. We present here the behavior of some of the most used protecting groups in peptide chemistry under experimental cleavage conditions, combining MgI2 with MW irradiation, using 2-Me-THF as a green solvent. In these experimental conditions, the benzyloxycarbonyl protecting group as well as the Merrifield resin can be re-considered in peptide chemistry.

Fmoc-OPhth, the reagent of Fmoc protection

Fmoc-OSu has been widely used for Fmoc protection of amino groups, especially amino acids, in solid phase peptide synthesis. However, it has been recognized that Fmoc-βAla-OH is formed as a by-product via the Lossen rearrangement during the reaction. Since we reconfirmed the formation of Fmoc-βAla-OH during the preparation of Fmoc-AA-OH by Fmoc-OSu, Fmoc-OPhth was designed and synthesized as a new Fmoc reagent to avoid the formation of Fmoc-βAla-OH. Furthermore, Fmoc protection by Fmoc-OPhth and Fmoc-SPPS were evaluated. The various Fmoc-amino acids prepared by Fmoc-OPhth were carried out in good yields and these are applicable in Fmoc-SPPS.