lysinoalanine

Lysinoalanine is a non-proteinogenic amino acid formed by crosslinking between lysine and dehydroalanine, yielding a characteristic C-C linked structure that contains both a lysine-derived side-chain amine and an alanine-derived backbone functionality. The molecule bears a free or derivatizable amino group(s) and a carboxylate/amide-forming site, enabling salt formation and coupling chemistry under standard amino acid conditions. Its stereochemical outcome is tied to the precursor dehydroalanine geometry and the reaction environment, so lysinoalanine is commonly handled as a defined stereochemical building block or as a mixture depending on synthetic origin. As a chemically stable yet functionally reactive amino acid crosslink motif, lysinoalanine serves as a research intermediate for studying amino acid conversion, protein modification pathways, and downstream analytical standards.

1. Protein Crosslinking Studies

Lysinoalanine is used in chemical biology and protein chemistry to model lysine-to-dehydroalanine crosslink formation that occurs during amino acid conversion and processing of proteinaceous materials. The lysine-derived side-chain amino functionality and the backbone carboxyl group allow derivatization to amides, activated esters, or labeled analogs that mimic the chemical handle present in crosslinked proteins. Incorporation of lysinoalanine-containing motifs into peptide substrates can support mechanistic studies of crosslink stability, hydrolysis susceptibility, and accessibility of modified residues under controlled conditions. Lysinoalanine thus functions as a chemically defined reference for amino acid crosslink chemistry and for mapping modification patterns in protein-focused investigations.

2. Peptide Substrate Design

Lysinoalanine is applied in peptide synthesis and peptide substrate design for generating defined crosslink-containing peptide fragments used in enzymology and reaction pathway probing. The amino acid backbone supports peptide coupling strategies, while the side-chain amine can be protected or selectively functionalized to control regioselective formation of amide bonds during solid-phase or solution-phase peptide assembly. Protecting-group logic can be used to differentiate the backbone carboxyl activation from the side-chain amine reactivity, enabling construction of lysinoalanine-bearing sequences or peptidomimetic linkers. Downstream, lysinoalanine-containing peptides can be employed as substrates or standards to assess how crosslink geometry influences recognition and reactivity in biochemical assays and synthetic methodology development.

3. Analytical Reference Standards

Lysinoalanine is utilized in analytical research as a reference compound for quantifying amino acid conversion products and crosslinked residues in processed proteins, hydrolysates, and reaction mixtures. The presence of amino and carboxyl functional groups enables derivatization for chromatographic detectability and mass spectrometric characterization, including formation of stable derivatives that improve ionization and peak assignment. Defined chemical identity supports method validation for targeted LC-MS/MS workflows aimed at measuring lysinoalanine formation and related modification markers. Lysinoalanine therefore serves as a key analytical building block for amino acid derivatization, method development, and crosslink profiling in biochemical and industrial feedstock studies.

4. Chemical Manufacturing Intermediates

Lysinoalanine is relevant to process chemistry and fine chemical synthesis as an intermediate for producing labeled standards, functionalized crosslink analogs, and downstream amino acid derivatives. The molecule's dual functional group set allows conversion into N-protected derivatives or activated forms that can be carried into subsequent coupling steps, supporting scalable preparation of peptide-building motifs and analytical reagents. Crosslink motif chemistry can also be leveraged to generate specialty chemical inputs for studying protein modification kinetics and for developing controlled model systems used in manufacturing-relevant quality assessment. Lysinoalanine thus supports industrially oriented amino acid derivatization routes where defined crosslink chemistry and reproducible analytical behavior are required.

5. Bioconjugation and Labeling

Lysinoalanine is used in biomolecule modification and bioconjugation workflows to introduce a defined crosslink-like amino acid handle onto peptides, polymers, or protein scaffolds. The side-chain amine and carboxyl functionality can be transformed into conjugation-ready derivatives, enabling coupling to activated surfaces, linkers, or detection tags while preserving the crosslink motif's chemical identity. Selective protection and controlled deprotection strategies can be applied to manage competing amine reactivity and to maintain consistent attachment sites for reproducible labeling. Lysinoalanine-derived conjugates can then serve as tools for chemical biology studies, crosslink mapping, and material-oriented functionalization where amino acid-based connection chemistry is required.

1. Relatedness of antibodies to peptides containing homocitrulline or citrulline in patients with rheumatoid arthritis

2. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes

3. Spatiotemporal delivery of nanoformulated liraglutide for cardiac regeneration after myocardial infarction

4. Investigating Potential Interactions Between Neurohypophyseal Peptides, their Drug Analogs, and Coagulation Factor VIII

5. Effect of Probiotic Lactobacillus plantarum on Streptococcus mutans and Candida albicans Clinical Isolates from Children with Early Childhood Caries