L-HomoPhenylalanine is a natural amino acid derivative classified as an aliphatic homolog of phenylalanine, featuring an amino acid backbone with a side chain extended by one methylene relative to phenylalanine and terminating in a benzyl-like phenyl group. The molecule contains a primary amino group and a carboxyl group, with the stereocenter indicated as L in the product name, and its side chain bears a hydrophobic aromatic functionality that can participate in π-related interactions in peptide environments. L-HomoPhenylalanine is used in peptide and protein-structure studies as a substrate for incorporating a phenylalanine homolog into synthetic sequences, supporting structure-activity and conformational investigations where side-chain length and hydrophobic/aromatic spacing are varied.
L-HomoPhenylalanine is an L-configured amino acid featuring an extended side chain relative to phenylalanine, with a stereogenic α-carbon bearing an amino group and a carboxylic acid. The molecule presents a benzyl-like aromatic ring at the terminus of a longer methylene chain, enabling hydrophobic and π-interaction patterns distinct from standard phenylalanine derivatives. The free amine and carboxylic acid can be selectively protected or converted into activated forms for peptide coupling, while the aromatic ring supports electrophilic substitution, oxidation, and cross-coupling chemistry depending on functionalization. As a chiral amino acid building block and synthetic intermediate, L-HomoPhenylalanine participates in stereochemically controlled derivatization and can be carried through protected amino acid strategies into downstream peptide and peptidomimetic constructs.
1. Peptide Synthesis
L-HomoPhenylalanine is used in peptide building block preparation where its L-stereochemistry supports formation of defined amide linkages during solid-phase or solution-phase peptide synthesis. The carboxylic acid can be converted to an activated ester or coupling-ready derivative, while the amino group is typically introduced under N-protection to prevent side reactions during chain elongation. The extended hydrophobic side chain influences local conformation and can be leveraged to tune helix propensity, receptor binding pockets, or protease recognition in peptide analogs. L-HomoPhenylalanine incorporation enables construction of sequence-defined peptides and peptidomimetics that retain aromatic functionality while varying side-chain length.
2. Side-Chain Functionalization
L-HomoPhenylalanine is applied in side-chain functionalization workflows that exploit the aromatic ring and the additional methylene units for controlled derivatization. The amino acid backbone supports orthogonal protection strategies, allowing selective transformation of the side-chain while maintaining compatibility with peptide coupling or subsequent deprotection steps. Aromatic modification routes can introduce halogens, alkoxy substituents, or handle-bearing substituents that support further coupling chemistry, including cross-coupling or nucleophilic aromatic substitution where appropriate. L-HomoPhenylalanine-derived intermediates can thus feed into libraries of functionalized amino acids and tailor-made peptide fragments for structure-guided molecular design.
3. Chiral Building Block Development
L-HomoPhenylalanine serves as a chiral amino acid intermediate for stereoselective synthesis of noncanonical amino acid derivatives and chiral ligands. The L-configuration at the α-carbon provides a stereogenic center that can be retained through protection, activation, and coupling steps, supporting downstream creation of chiral amide, ester, or heteroatom-linked derivatives. The free carboxyl functionality can be masked as an ester or converted to a carboxamide, while the amino group can be protected to enable selective transformations at the aromatic ring or side-chain terminus. L-HomoPhenylalanine can be employed to generate enantiopure intermediates for fine chemical synthesis and stereocontrolled manufacturing of amino acid-derived scaffolds.
4. Chemical Biology Labeling
L-HomoPhenylalanine is utilized in chemical biology and biomolecule modification strategies where aromatic and hydrophobic side-chain features assist in positioning probes within protein microenvironments. The amino acid framework can be incorporated into peptide tags or recognition motifs, and the carboxyl/amine functionality supports conversion into conjugation-ready handles after suitable protection and activation. Side-chain derivatization can introduce clickable or affinity-bearing groups that enable labeling workflows targeting proteins, peptides, or other biomolecular assemblies under controlled chemistries. L-HomoPhenylalanine-based constructs support generation of labeling reagents and analytical probes used to map molecular interactions and study binding determinants.
5. Process Chemistry Intermediate
L-HomoPhenylalanine is applied as a process chemistry intermediate for industrial synthesis of amino acid derivatives that require reliable handling of functional groups and stereochemical integrity. The presence of both an amino and a carboxylic acid supports scalable protection-group selection, enabling controlled conversion into coupling-ready forms for subsequent manufacturing steps. The aromatic side chain and extended methylene spacer can be carried through multi-step routes to produce specialty fine chemicals, including peptidomimetic fragments and functionalized aromatic-containing intermediates. L-HomoPhenylalanine thus functions as a chiral feedstock for downstream chemical manufacturing where amino acid chemistry and intermediate robustness are central to route design.
6. SAR Studies And Peptidomimetics
L-HomoPhenylalanine is employed in structure-activity relationship studies and peptidomimetic construction where side-chain length relative to phenylalanine can modulate binding geometry and conformational preferences. The L-amino acid backbone supports systematic substitution patterns by enabling N-protection, C-terminal activation, and iterative coupling into analog series. The aromatic ring contributes to hydrophobic contacts and π-interactions, while the extra methylene unit can alter distance to adjacent functional groups in a binding site. L-HomoPhenylalanine incorporation enables generation of stereochemically defined peptide analogs and SAR-focused libraries that inform medicinal chemistry optimization without requiring departure from amino acid-compatible synthesis logic.
2. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die
3. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More