951695-85-5

Basic information

• Product Name: FMOC-LYS(BOC)(ME)-OH
• Synonyms: N-ALPHA-(9-FLUORENYLMETHYLOXYCARBONYL)-N-EPSILON-TERT-BUTYLOXYCARBONYL-N-EPSILON-METHYL-L-LYSINE;N-ALPHA-(9-FLUORENYLMETHYLOXYCARBONYL)-N-EPSILON-T-BUTYL-OXYCARBONYL-N-EPSILON-METHYL-L-LYSINE;N-ALPHA-(9-FLUORENYLMETHOXYCARBONYL)-N-EPSILON-T-BUTOXYCARBONYL-N-EPSILON-METHYL-L-LYSINE;N-ALPHA-FMOC-N-EPSILON,EPSILON-T-BOC-METHYL-L-LYSINE;N-ALPHA-FMOC-N-EPSILON-METHYL-N-EPSILON-T-BOC-L-LYSINE;FMOC-LYS(BOC)(ME)-OH;FMOC-LYS(ME,BOC)-OH;FMOC-LYSINE(BOC)(ME)-OH
• CAS NO: 951695-85-5
• Molecular Formula: C₂₇H₃₄N₂O₆
• Molecular Weight: 482.57
• Product Categories: amino acids
• Mol File: 951695-85-5.mol
• Article Data: 4

Chemical Properties

• Melting Point: 85-87℃
• Boiling Point: 665.36 °C at 760 mmHg
• Flash Point: 356.197 °C
• Appearance: /
• Density: 1.200
• Storage Temp.: -15°C
• PKA: 3.88±0.21(Predicted)
• CAS DataBase Reference: FMOC-LYS(BOC)(ME)-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-LYS(BOC)(ME)-OH(951695-85-5)
• EPA Substance Registry System: FMOC-LYS(BOC)(ME)-OH(951695-85-5)

Safety Data

• Hazard Codes: Xi
• WGK Germany: WGK 2 water endangering
• Hazardous Substances Data: 951695-85-5(Hazardous Substances Data)

Usage

Description

Fmoc-lys (BOC) (ME)-OH is a kind of protected form of lysine. Lysine is double-protected by butyloxycarbonyl (BOC) and 9H-fluoren-9-ylmethoxycarbon (FMOC). It is a derivative for the introduction of monomethyl-lysine during Fmoc SPPS. Coupling can be carried out using any standard activation method. The Boc protecting group can be removed through the TFA-mediated cleavage reaction. As a kind of protected amino acid, it is an important intermediate in various fields such as peptide synthesis, asymmetric synthesis, medicinal chemistry as well as polymer chemistry.

Uses

Heterochromatin protein 1 (HP1) depends on trimethylation of H3 Lys 9; aggregation of chromatines depends on Lys methylation Fmoc-Lys(Boc, Me)-OH is useful for preparing monomethylated histone fragments utilized in studying the regulatory roles of methylated histones. Fmoc-Lys(Boc,Me)-OH can be coupled using standard activating procedures. The Boc group on the side epsilon nitrogen atom is removed with TFA, usually at the same time as the peptide is cleaved from the resin. Fmoc-Lys(Boc, Me)-OH is a novel derivative for the introduction of monomethyl-lysine during Fmoc SPPS. Coupling can be carried out using any standard activation method. Removal of the Boc protecting group occurs during the course of the TFA-mediated cleavage reaction.

General Description

Fmoc protected N-methylated lysine

References

http://www.chempep.com/ChemPep_Products2_Fmoc-Amino-Acid_Fmoc-Lys_Boc_Me_-OH.htm https://en.wikipedia.org/wiki/Peptide_synthesis Tung, C. L., et al. "A fluorogenic probe for recognizing 5-hydroxylysine inspired by serine/threonine ligation. " Chemical Communications 50.40(2014):5298-300.

Upstream product

• 1238313-29-5 N^α-Ac-N^ε-(Boc, methyl)-DL-lysine 
• 1190081-84-5 N^ε-tert-butyl-oxycarbonyl-N^ε-methyl-L-lysine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 5183-27-7 6-bromo-2-acetamido-2-ethoxycarbonyl-hexanoic acid ethyl ester 
• 757233-08-2 2-acetylamino-2-(4-bromo-butyl)-malonic acid monoethyl ester 
• 757233-09-3 N-acetyl-DL-2-amino-6-bromohexanoic acid ethyl ester 
• 1238313-27-3 N^α-Ac-N^ε-(Boc, methyl)-DL-lysine ethyl ester 
• 24424-99-5 di-tert-butyl dicarbonate 
• 951695-86-6 N-fluorenylmethoxycarbonyl-N'-methyl-L-lysine 
• 139262-23-0 9-fluorenylmethoxycarbonyl-L-alanine hydrochloride 
• 111061-54-2 N^α-Fmoc-N^ε-Trt-Lys 
• 146549-21-5 2-(9H-fluoren-9-ylmethoxycarbonylamino)-pent-4-enoic acid 
• 169268-90-0 3-N-tert-butoxycarbonylamino-N-methyl-1-propene 

Downstream Products

• 1190081-84-5 N^ε-tert-butyl-oxycarbonyl-N^ε-methyl-L-lysine 
• 1598424-87-3 N^ε-(Boc, methyl)-L-lysine-MCA 
• 1598424-92-0 N^α-Fmoc-N^ε-(Boc, methyl)-L-lysine-MCA 
• 951695-86-6 N-fluorenylmethoxycarbonyl-N'-methyl-L-lysine 
• 1451046-69-7 C₂₅H₃₂N₂O₄*ClH 
• 1451145-31-5 C₂₅H₃₂N₂O₄ 

Relevant articles and documents

Preparation method of N epsilon-tert-butoxycarbonyl-N alpha-fluorenylmethoxycarbonyl-N epsilon-methyl-lysine

The invention discloses a preparation method of N epsilon-tert-butoxycarbonyl-N alpha-fluorenylmethoxycarbonyl-N epsilon-methyl-lysine. The preparation method comprises the following steps: taking N alpha-fluorenylmethoxycarbonyl-lysine hydrochloride as a raw material, performing alkylation with halide (R-X) under alkaline conditions, performing reductive amination on alkylate in an aqueous formaldehyde solution to introduce methyl, removing an R group of a reductive amination product under acidic conditions, then introducing a t-butyloxycarboryl (BOC) protecting group under alkaline conditions and performing re-crystallization treatment to obtain a product. The preparation method disclosed by the invention is simple in synthetic route and mild in reaction conditions, and the next-step reaction can be directly carried out after an intermediate is simply washed and concentrated. The reaction yield in each step is close to quantification, the total yield can reach above 80 percent, the purity of a final product exceeds 98 percent, and a safe and efficient synthetic route is provided for the preparation of the N epsilon-tert-butoxycarbonyl-N alpha-fluorenylmethoxycarbonyl-N epsilon-methyl-lysine.

Analysis of JmjC Demethylase-Catalyzed Demethylation Using Geometrically-Constrained Lysine Analogues

The dynamic post-translational modifications of histones play important roles in the regulation of transcription in animals. The demethylation of Nε-methyl lysine residues in the N-terminal tail of histone H3 is catalyzed by demethylases, of which the largest family is the ferrous iron and 2-oxoglutarate dependent demethylases (JmjC KDMs), which catalyze demethylation via initial hydroxylation of the N-methyl groups. We report studies on the conformational requirements of the JmjC KDM substrates using N-methylated lysine analogues prepared by metathesis reactions of suitably protected N-allylglycine. The results support the proposed requirement for a positively charged Nε-amino group in JmjC KDM catalysis. Demethylation of a trans-C-4/C-5 dehydrolysine substrate analogue was observed with representative KDM4 subfamily members KDM4A, KDM4B and KDM4E, and KDM7B, which are predicted, based on crystallographic analyses, to bind the Nε-methylated lysine residue in different conformations during catalysis. This information may be useful in the design of JmjC KDM selective inhibitors.