Fmoc-L-Val-OH
- Price: ¥1000/Kg
- Createtime: 2024-09-04
- Updatetime: 2024-09-04
Product Details
CAS |
68858-20-8
|
PU |
99%
|
MF |
C20H21NO4
|
EINECS |
272-515-0
|
Chemical Name: Fmoc-L-Val-OH
Molecular Formula: C20H21NO4
Molecular Weight: 337.40 g/mol
Overview
Fmoc-L-Val-OH is a protected amino acid derivative extensively used in solid-phase peptide synthesis (SPPS). This compound features L-valine, a branched-chain amino acid, with its amino group protected by the Fmoc (9-fluorenylmethyloxycarbonyl) group. The Fmoc group is crucial for controlling the peptide synthesis process by preventing unwanted reactions and ensuring the precise incorporation of valine into peptide chains.
Importance in Peptide Synthesis
The Fmoc strategy is widely preferred in SPPS due to its efficiency and mild deprotection conditions, typically involving a base like piperidine. Fmoc-L-Val-OH is particularly important for synthesizing peptides that include valine residues. Valine's branched aliphatic side chain contributes to the hydrophobic nature of the peptide, which can significantly influence peptide folding and stability.
Valine is one of the essential amino acids and plays a critical role in protein structure and function. Its side chain is involved in hydrophobic interactions that help stabilize protein and peptide structures. By incorporating valine into peptides, researchers can study the effects of hydrophobic interactions and create peptides with specific structural and functional properties.
Applications
Fmoc-L-Val-OH is used in the synthesis of a wide variety of peptides, from short sequences to complex proteins. Peptides containing valine residues are valuable in several fields, including drug development, enzyme studies, and biomaterial creation. The ability to incorporate valine precisely allows for the design of peptides with specific sequences and characteristics.
Valine-rich peptides are important in studying protein folding, hydrophobic interactions, and stability. For instance, valine is often found in the interior of proteins, where it contributes to the hydrophobic core that stabilizes protein structures. Synthetic peptides containing valine can be used to investigate protein-protein interactions, develop peptide-based therapeutics, and design biomaterials with tailored properties.
Handling and Storage
Fmoc-L-Val-OH should be handled with care, as with other chemical reagents. It is typically stored in a cool, dry place, away from light and moisture, to prevent degradation. Proper storage conditions are essential to maintain the stability and reactivity of the compound, ensuring its suitability for peptide synthesis.
Conclusion
Fmoc-L-Val-OH is a fundamental reagent in peptide synthesis, enabling the precise incorporation of L-valine into peptide sequences. Its role in SPPS is crucial for creating peptides with specific hydrophobic properties and functional activities, making it a valuable tool in advancing research in biochemistry, molecular biology, and drug development. By using Fmoc-L-Val-OH, scientists can design and synthesize peptides that contribute to therapeutic applications, structural studies, and a deeper understanding of protein interactions and functions.