How to get Fmoc-Val-OH?

Fmoc-Val-OH
CAS No.:68858-20-8
Molecular formula:C20H21NO4
Molecular weight:339.4
Purity(HPLC):98.5% min.
Fmoc-Val-OH is white crystalline powder with melting point of 143~146 ℃. Specific rotation(20/D) is -17o (c=1, DMF).
Fmoc-Val-OH is a solid phase peptide synthesis (SPPS)that has been the most efficient method for the preparation of peptides since its introduction in 1963 by Bruce Merrifield. The t-Boc amino acid derivatives had been used dominantly for the SPPS until the Fmoc chemistry was introduced to overcome the t-Boc chemistry problems, repetitive TFA treatment which might catalyze the side reactions and cleave the peptide chain prematurely. In Fmoc synthesis, the growing peptide is subjected to mild base treatment using piperidine to remove the Fmoc group, and TFA is required only for the final deprotection and cleavage from the resin. The comparison experiments  between Fmoc and t-Boc approache indicate that Fmoc chemistry is more reliable and tends to give the desired peptides in better purities.
Attaching the first amino acid to the resin requires special protocols, and racemization of the Fmoc-amino acid can result when special precautions are not taken. Using pre-loaded Fmoc-amino acid Wang resins save time and effort.
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What is Fmoc-Val-OH?

Fmoc-Val-OH
CAS No.:68858-20-8
Molecular formula:C20H21NO4
Molecular weight:339.4
Purity(HPLC):98.5% min.
Appearance:White crystalline powder
Melting point:143~146 ℃
Specific rotation(20/D): -17o (c=1, DMF
The Fmoc group of Fmoc amino acids is acid stable but is removed with a base through a β-elimination reaction. The Fmoc group of Fmoc amino acids is less labile to primary amines than secondary amines, thus minimizing premature Fmoc deprotection by the N-terminal amine of the deprotected peptide intermediate. Fmoc amino acids are typically deprotected using piperidine, which also scavenges the reactive dibenzofulvene byproduct of Fmoc cleavage. In cases of sluggish deblocking of Fmoc amino acids, DBU may be used to remove the protecting group with added piperidine to scavenge the dibenzofulvene byproduct. DBU promotes aspartimide formation, and it should be used cautiously when the peptide contains aspartic acid residues. Alternatively in difficult sequences, using piperidine/DMF (1:4) with mild heating at 45°C can be effective
By the early 1990s, Fmoc amino acids were as popular as Boc amino acids for peptide synthesis. The Fmoc amino acid protecting group was developed by Carpino in 1970 (Carpino and Han, J. Am. Chem. Soc. 1970, 92, 5748-9), and he soon developed solid phase peptide synthesis protocols utilizing Fmoc amino acids. The strong UV absorbance of the Fmoc amino acids and the Fmoc cleavage byproducts allow solid phase peptide synthesis reactions to be easily monitored by photometry. In the late 1970s, automated peptide synthesizers with reaction monitoring capabilities based on measuring Fmoc absorption were introduced. In spite of their high cost, Fmoc amino acids gained popularity. By the 1980s, Fmoc amino acids were very popular. Adding to the popularity of Fmoc amino acids in solid phase peptide synthesis is that TFA-labile resins could be used, thus eliminating the need to utilize HF and special HF cleavage equipment. As the popularity and use of Fmoc amino acids increased, prices of Fmoc amino acids dropped. Since then, Fmoc amino acids have quickly become one of the standards for solid phase peptide synthesis.
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Specifications of Fmoc-Val-OH

Fmoc-Val-OH
CAS No.:68858-20-8
Molecular formula:C20H21NO4
Molecular weight:339.4
Specification of Fmoc-Val-OH
Purity(HPLC):98.5% min.
Appearance:White crystalline powder
Melting point:143~146 ℃
assay 98%
optical activity  [α]20/D −17°, c = 1 in DMF
mp 143-145 °C(lit.)
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