Study on the Chemical Properties and Applications of H-Lys-Ala-OH (Lysyl-Alanine Dipeptide)
Chemical Structure and Basic Properties
H-Lys-Ala-OH is a dipeptide compound formed by the connection of lysine (Lys) and alanine (Ala) through peptide bonds. From a molecular structure perspective, this dipeptide has a lysine residue at its N-terminus, with its α-amino group forming an amide bond (peptide bond) with the α-carboxyl group of alanine via dehydration condensation reaction. The side chain of lysine contains four methylene groups and one terminal amino group, which gives this dipeptide a typically positive charge under physiological conditions. Alanine is one of the simplest amino acids, with its side chain being just a methyl group; this affects to some extent the spatial conformation and hydrophobicity of the dipeptide.
The molecular formula for this compound is C₉H₂₀N₄O₃, with a molecular weight of 201.25 Daltons. Due to the presence of lysine residues, the entire molecule exhibits basic characteristics. Although literature does not explicitly record its precise isoelectric point, it can be inferred from pKa values that it should fall within an alkaline range. This compound's CAS registration number is 17043-71-9, commonly classified in chemical databases as a simple linear dipeptide.
Physicochemical Property Analysis
From solubility perspectives, H-Lys-Ala-OH displays typical zwitterionic properties in aqueous solution due to both ionizable amino and carboxylic groups present in its structure; thus solubility significantly depends on pH levels. Under acidic conditions, ε-amino groups from lysine’s side chain become protonated causing overall positive charge for molecules; conversely under alkaline conditions deprotonation occurs at α-carboxylic acid leading to negative charges overall for molecules. This pH-dependent charge characteristic results in significant differences in solubility behavior across various buffer systems.
Experiments indicate limited solubility for this dipeptide in pure water but can be significantly enhanced by adding appropriate organic acids (such as 10-30% acetic acid) or strong acids (like trifluoroacetic acid). Such dissolving properties are closely related to basic amino acid residues existing within their molecular structures. In solid-state form compounds usually exist as white crystalline powders recommended stored away from light below -20°C ensuring stability while solutions should avoid repeated freeze-thaw cycles suggesting low-temperature storage after aliquoting.
Synthesis Methods & Process Optimization
Synthesis methods for H-Lys-Ala-OH may utilize traditional liquid-phase peptide synthesis techniques or modern solid-phase peptide synthesis technologies involving protecting strategies like Boc or Fmoc used during liquid phase routes before employing coupling agents such as DCC or HBTU facilitating condensation reactions followed by deprotection processes yielding target peptides eventually obtained post-reaction completion. In recent years advancements made regarding solid-phase peptide synthesis have greatly improved efficiency rates achieved through anchoring first amino-acid onto resin then sequentially undergoing deprotection/coupling steps ultimately releasing target peptides off resin via cleavage reactions enhancing yield alongside purification operations’ convenience emphasizing importance regardless chosen method where final product purification remains crucial often requiring high-performance liquid chromatography(HPLC).
Biochemical Research Value
As one among simplest known di-peptides , H-Lys-Ala-OHs holds considerable significance foundational biochemical research purposes . Primarily serving ideal model compounds investigating mechanisms behind formation hydrolysis occurring between peptide bonds studying stability factors influencing these interactions such as varying temperature,pH ionic strength etc.. Secondly acting models examining interactions taking place amongst different types Amino Acids particularly focusing upon positively charged Lysines effects against other oppositely charged moieties could provide insights into electrostatic attractions happening therein . in protein folding studies simple Di-Peptides serve frequently referenced objects comparing conformational changes experienced when placed diverse solvent environments aiding comprehension concerning more complex polypeptides folding behaviors furthermore since Lysin serves essential role human body’s nutritional requirements understanding absorption metabolism patterns observed respective forms might prove beneficial towards elucidating digestive uptake mechanisms underlying proteins previously shown certain Di-Peptides exhibit higher absorption efficiencies compared free-form Amino Acids presenting new ideas supplement designs addressing nutrient needs effectively . nExisting studies reveal several potential applications spanning medicinal food science material sciences encompassing varied fields wherein prospects warrant exploration including utilization intermediates structural modules drug development functional ingredients specialized medical formulations improving dietary supplementation efficacies exploring novel self assembling supramolecular architectures creating biocompatible materials delivery systems exploiting versatile functionalities available given nature comprising constituent components enriching current knowledge base surrounding practical implications stemming thereof providing future directions targeted investigations aligning scientific endeavors pursuing innovative breakthroughs delivering impactful contributions society comprehensively altogether reflecting necessity continued inquiry pursuit unearthing valuable discoveries underpinning health wellness sustainability realms contributing holistic advancement global communities universally.