N-Fmoc-N-Methyl-beta-alanine

≥97%

Reagent Code: #76509
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CAS Number 172965-84-3

science Other reagents with same CAS 172965-84-3

blur_circular Chemical Specifications

scatter_plot Molecular Information
Weight 325.36 g/mol
Formula C₁₉H₁₉NO₄
badge Registry Numbers
MDL Number MFCD01861327
inventory_2 Storage & Handling
Storage room temperature, dry

description Product Description

This compound is primarily utilized in the field of peptide synthesis, where it serves as a building block for constructing peptides with specific structural features. Its Fmoc (fluorenylmethyloxycarbonyl) protecting group is particularly advantageous in solid-phase peptide synthesis, allowing for selective deprotection and subsequent coupling reactions. The N-methyl group introduces conformational constraints, which can enhance the stability and biological activity of the resulting peptides. This makes it valuable in the development of peptide-based drugs, where modifying the peptide backbone can improve pharmacokinetic properties and target specificity. Additionally, it is employed in research to study peptide structure-activity relationships, aiding in the design of novel therapeutic agents.

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Size Availability Unit Price Quantity
inventory 1g
10-20 days ฿954.00
inventory 250mg
10-20 days ฿387.00
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N-Fmoc-N-Methyl-beta-alanine
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This compound is primarily utilized in the field of peptide synthesis, where it serves as a building block for constructing peptides with specific structural features. Its Fmoc (fluorenylmethyloxycarbonyl) protecting group is particularly advantageous in solid-phase peptide synthesis, allowing for selective deprotection and subsequent coupling reactions. The N-methyl group introduces conformational constraints, which can enhance the stability and biological activity of the resulting peptides. This makes

This compound is primarily utilized in the field of peptide synthesis, where it serves as a building block for constructing peptides with specific structural features. Its Fmoc (fluorenylmethyloxycarbonyl) protecting group is particularly advantageous in solid-phase peptide synthesis, allowing for selective deprotection and subsequent coupling reactions. The N-methyl group introduces conformational constraints, which can enhance the stability and biological activity of the resulting peptides. This makes it valuable in the development of peptide-based drugs, where modifying the peptide backbone can improve pharmacokinetic properties and target specificity. Additionally, it is employed in research to study peptide structure-activity relationships, aiding in the design of novel therapeutic agents.

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