Chemical Name: Fmoc-L-Ile-OH
Molecular Formula: C21H23NO4
Molecular Weight: 339.42 g/mol

Overview
Fmoc-L-Ile-OH is a protected amino acid derivative widely utilized in solid-phase peptide synthesis (SPPS). This compound features L-isoleucine, 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, preventing unwanted side reactions, and ensuring the precise incorporation of isoleucine into peptide chains.

Importance in Peptide Synthesis
The Fmoc strategy is preferred in SPPS due to its efficiency and mild deprotection conditions, usually achieved with a base like piperidine. Fmoc-L-Ile-OH is particularly significant for synthesizing peptides that include isoleucine residues. Isoleucine, with its branched aliphatic side chain, contributes to the hydrophobic nature of peptides, influencing their folding, stability, and interactions.

Isoleucine is an essential amino acid with a side chain that participates in hydrophobic interactions, which are vital for stabilizing protein and peptide structures. By incorporating isoleucine into peptides, researchers can study the effects of hydrophobic interactions and design peptides with specific structural and functional characteristics.

Applications
Fmoc-L-Ile-OH is extensively used in the synthesis of peptides requiring the presence of isoleucine residues. These peptides are valuable in a range of fields, including drug development, enzyme studies, and biomaterial creation. The precise incorporation of isoleucine allows for the development of peptides with tailored properties and functionalities.

Isoleucine-rich peptides are important for studying protein folding, stability, and hydrophobic interactions. For example, isoleucine is often found in the interior of proteins, contributing to the hydrophobic core that stabilizes their structures. Synthetic peptides containing isoleucine can be used to investigate protein-protein interactions, develop peptide-based therapeutics, and design biomaterials with specific hydrophobic properties.

Handling and Storage
Fmoc-L-Ile-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-Ile-OH is a crucial reagent in peptide synthesis, enabling the precise incorporation of L-isoleucine into peptide sequences. Its role in SPPS is vital for creating peptides with specific hydrophobic properties and functional activities, making it an invaluable tool in advancing research in biochemistry, molecular biology, and drug development. By using Fmoc-L-Ile-OH, scientists can design and synthesize peptides that contribute to therapeutic applications, structural studies, and a deeper understanding of protein interactions and functions.