H-Lys(Z)-OBzL.HCl is a specialized peptide derivative used in peptide synthesis and biochemical research. It features the lysine (Lys) residue with a protected side chain, benzyl ester (OBzL) modification, and is provided as a hydrochloride salt (HCl). This compound is notable for its role in controlling peptide reactivity and stability, particularly in the context of solid-phase peptide synthesis (SPPS) and peptide modification.

Structure and Components:
Lysine (Lys): Lysine is an essential amino acid with a positively charged amino group in its side chain. This property makes lysine a key player in ionic interactions and protein folding. In H-Lys(Z)-OBzL.HCl, the side chain of lysine is protected by a Z (benzyloxycarbonyl) group, which prevents side chain reactions during peptide synthesis.

Z Protection Group: The Z group (benzyloxycarbonyl) is a protective group used to shield the amino group of lysine's side chain during peptide synthesis. The Z group is stable under basic conditions and can be removed using hydrogenolysis or other specific deprotection methods, revealing the free amino group of lysine for further chemical reactions or peptide assembly.

Benzyl Ester (OBzL): The benzyl ester (OBzL) modification is attached to the carboxyl terminus of the lysine residue. This ester group protects the carboxyl function during synthesis and can be selectively deprotected to reveal the carboxyl group for subsequent reactions or peptide coupling.

Hydrochloride Salt (HCl): The hydrochloride salt form (HCl) is used to stabilize the peptide derivative and enhance its solubility in aqueous solutions. This form is particularly useful for handling and dissolving the peptide in various chemical and biological experiments.

Applications:
Peptide Synthesis: H-Lys(Z)-OBzL.HCl is used in peptide synthesis where protection of the lysine side chain and carboxyl terminus is required. The Z group and OBzL modification enable controlled assembly of peptides, preventing side reactions and allowing for precise sequence construction.

Functional Studies: The controlled reactivity of the lysine side chain in H-Lys(Z)-OBzL.HCl makes it valuable for studying peptide interactions and functional properties. The ability to deprotect and modify lysine residues allows researchers to investigate the role of lysine in various biological processes.

Pharmaceutical Development: This compound can be employed in drug design to create peptides with specific functional groups or modified lysine residues. The Z and OBzL protection strategies help in designing peptides with optimized therapeutic properties and stability.

Biotechnology: In biotechnology, H-Lys(Z)-OBzL.HCl is used in the development of peptide-based materials and biosensors. The protected lysine residue can be leveraged to create materials with specific interactions or properties, including selective binding or enhanced stability.

Conclusion:
H-Lys(Z)-OBzL.HCl is a crucial peptide derivative in peptide chemistry, offering a combination of protective and functional groups. Its role in solid-phase peptide synthesis, functional studies, and pharmaceutical development underscores its importance in creating peptides with tailored properties. By utilizing H-Lys(Z)-OBzL.HCl, researchers and developers can design peptides with precise structural and functional characteristics, advancing scientific research and various industrial applications.