H-Lys(2-chloro-Z)-OBzl · HCl

H-Lys(2-chloro-Z)-OBzl · HCl is a protected lysine derivative in which the α-amino group is protected as a Z-type carbamate (Z = benzyloxycarbonyl), while the side-chain terminus is masked as a benzyl ester (OBzl) and bears a 2-chloro substituent on the side-chain carbon framework. The molecule contains a defined stereochemical lysine backbone with a free carboxyl-derived functionality converted to an ester, and it is supplied as the hydrochloride salt, which increases handling stability and can improve compatibility with acid-mediated protection/deprotection workflows. The presence of the benzyloxycarbonyl group provides a robust N-protecting strategy for peptide coupling chemistry, whereas the benzyl ester can be selectively removed under hydrogenolysis conditions to regenerate a carboxylate for downstream transformations. The 2-chloro functionality introduces a reactive electrophilic handle that can participate in nucleophilic substitution or serve as a precursor for further side-chain elaboration, making the compound suitable as a chiral intermediate for amino acid derivatization and peptide-related scaffold construction.

1. Protected Amino Acids

H-Lys(2-chloro-Z)-OBzl · HCl is used in protected amino acid synthesis workflows where orthogonal protection patterns are required for stepwise assembly. The Z-protected α-amine and the benzyl ester C-terminus provide chemically distinct functional groups that can be carried through peptide coupling steps without premature deprotection. The hydrochloride salt form helps maintain the protonated amine state during handling and can support controlled deprotection sequences when designing protected amino acid intermediates. The installed 2-chloro side-chain element can be retained during peptide building and later converted into additional functional groups, enabling targeted amino acid derivatization strategies for research-grade peptide building block preparation.

2. Peptide Synthesis

H-Lys(2-chloro-Z)-OBzl · HCl is applicable to peptide synthesis as a lysine-based building block designed for incorporation into protected peptide fragments. The Z-carbamate N-protection supports standard amide bond formation at the α-position while the benzyl ester C-terminus can be manipulated to match the intended peptide end-group, including conversion to a free acid for iterative coupling. The 2-chloro substituent on the lysine side-chain can be used to introduce a halogenated motif into peptide sequences, supporting structure-activity relationship studies and enabling later side-chain functionalization after assembly. The salt form and benzylic protecting groups align well with common protecting-group strategies used in peptide chemistry, supporting downstream generation of modified peptide analogs and peptidomimetic scaffolds.

3. Side-Chain Functionalization

H-Lys(2-chloro-Z)-OBzl · HCl serves as a chiral intermediate for side-chain functionalization where the 2-chloro group acts as a synthetic handle for nucleophilic substitution chemistry. The protected α-amine and esterified carboxyl group allow the molecule to undergo side-chain transformations without uncontrolled amide hydrolysis or carboxylate interference under many derivatization conditions. The benzyl ester can be deprotected to reveal a carboxylic acid for subsequent coupling or for preparing derivatives such as amides, mixed anhydrides, or activated esters. The resulting functionalized lysine derivatives can be used to generate electrophile-bearing or substituted side-chain analogs for chemical biology research, peptide analog libraries, and process chemistry intermediate preparation.

4. Chemical Biology Probes

H-Lys(2-chloro-Z)-OBzl · HCl can be applied in chemical biology research for constructing lysine-containing labeling handles and reactive peptide analogs. The halogenated side-chain motif provides a site for post-assembly modification, enabling the preparation of probes that can be further transformed into nucleophilic-reactive or affinity-tag-compatible structures. The Z-protected amine and benzyl ester enable incorporation into peptide-like backbones while maintaining functional group integrity during scaffold construction. The hydrochloride salt form supports consistent handling of the amino acid derivative as a protected intermediate, supporting downstream formation of modified biomolecule conjugation reagents and analytical standards derived from amino acid chemistry.

5. Pharmaceutical Intermediate Preparation

H-Lys(2-chloro-Z)-OBzl · HCl is suitable for pharmaceutical intermediate preparation where protected lysine derivatives are required for controlled synthesis of peptidomimetic or peptide-like intermediates. The orthogonal protection scheme, combining a carbamate-protected amine with a benzyl ester C-terminus, supports manufacturing route design by allowing selective deprotection steps aligned with downstream coupling or activation chemistry. The 2-chloro substituent can be carried through early stages as a defined chemical functionality and then converted into alternative side-chain groups to tune physicochemical properties of the intermediate. The compound's structure therefore supports fine chemical synthesis workflows that rely on stereochemically defined amino acid building blocks and predictable protecting-group behavior for scalable intermediate generation.

1. High fat diet and GLP-1 drugs induce pancreatic injury in mice

2. Myotropic activity and immunolocalization of selected neuropeptides of the burying beetle Nicrophorus vespilloides (Coleoptera: Silphidae)

3. Myotropic activity of allatostatins in tenebrionid beetles

4. Genetic, cellular, and structural characterization of the membrane potential-dependent cell-penetrating peptide translocation pore

5. An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I