Chemical Name: Fmoc-L-Ala-OH
Molecular Formula: C19H21NO4
Molecular Weight: 315.38 g/mol

Overview
Fmoc-L-Ala-OH is a protected amino acid derivative extensively used in solid-phase peptide synthesis (SPPS). This compound features L-alanine, a non-essential amino acid, with its amino group protected by the Fmoc (9-fluorenylmethyloxycarbonyl) group. The Fmoc group is crucial for controlling the peptide synthesis process, preventing undesired side reactions and ensuring the precise incorporation of alanine into peptide chains.

Importance in Peptide Synthesis
The Fmoc strategy is widely preferred in SPPS due to its efficiency and mild deprotection conditions, typically using a base such as piperidine. Fmoc-L-Ala-OH is particularly important for incorporating alanine residues into peptides. Alanine, with its simple aliphatic side chain, is a fundamental building block in peptide synthesis and is often used to study the effects of hydrophobic interactions on protein structure and function.

Alanine's non-reactive side chain makes it a versatile component in peptides, allowing researchers to create sequences with varying hydrophobic properties. Its small size and non-polar nature enable it to fit into protein cores and influence peptide folding and stability. Additionally, alanine is frequently used as a control or reference in peptide synthesis and structural studies.

Applications
Fmoc-L-Ala-OH is used in the synthesis of a wide variety of peptides, from short sequences to larger proteins. Peptides containing alanine residues are important in numerous applications, including drug development, enzyme studies, and the creation of biomaterials. The ability to incorporate alanine precisely allows researchers to design peptides with specific sequences and functional properties.

Alanine-rich peptides are often used to study protein folding and stability. In addition, alanine is frequently employed in the design of peptide libraries and as a building block in the development of peptide-based drugs. Its role as a control residue in structural studies helps in understanding the influence of hydrophobic interactions and side-chain effects on peptide and protein behavior.

Handling and Storage
Fmoc-L-Ala-OH should be handled with care, similar to 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-Ala-OH is a fundamental reagent in peptide synthesis, enabling the precise incorporation of L-alanine 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-Ala-OH, scientists can design and synthesize peptides that contribute to therapeutic applications, structural studies, and a deeper understanding of protein interactions and functions.