997-20-6

Usage

Uses

Used in Biomaterials:
LYS-LYS-LYS-LYS is used as a building block for creating biomaterials due to its repetitive lysine sequence, which can contribute to the development of materials with specific properties.
Used in Drug Delivery:
LYS-LYS-LYS-LYS is used as a carrier in drug delivery systems for its potential as a cell-penetrating peptide, allowing for efficient transport of therapeutic agents into target cells.
Used in Antimicrobial Agents:
LYS-LYS-LYS-LYS is used as a component in the development of antimicrobial agents, leveraging its multiple lysine residues to enhance its antimicrobial properties.
Used in Research:
LYS-LYS-LYS-LYS is used as a versatile tool in biomedical and materials science research for its potential applications in various fields, including tissue engineering, regenerative medicine, and the development of new materials with unique characteristics.

InChI:InChI=1/C24H50N8O5/c25-13-5-1-9-17(29)21(33)30-18(10-2-6-14-26)22(34)31-19(11-3-7-15-27)23(35)32-20(24(36)37)12-4-8-16-28/h17-20H,1-16,25-29H2,(H,30,33)(H,31,34)(H,32,35)(H,36,37)

Upstream product

• 56-86-0 L-glutamic acid 
• 657-27-2 L-Lysine hydrochloride 
• 142354-67-4 L-lysine n-hexyl ester di-p-toluene sulfonate 
• 95839-39-7 L-lysine n-butyl ester di-p-toluene sulfonate 
• 3844-53-9 L-lysine ethyl ester dihydrochloride 

Relevant academic research and scientific papers

Modelling of prebiotic synthesis and selection of peptides under isothermal conditions and thermal cycling mode

The model peptide synthesis from mixtures of amino acids was carried out under the thermal cycling and isothermal modes. The compositions of the obtained mixtures of products and the primary amino acid sequence of the synthesized peptides were determined by Fourier transform ion cyclotron resonance mass spectrometry and tandem mass spectrometry in combination with high-performance liquid chromatography with the application of de novo sequencing of the synthesized products. The processes of abiogenous synthesis of peptides were shown to occur under relatively mild temperature conditions and give a substantially less number of peptides as compared with the possible statistical set. The evolution of the system takes place in the process of the synthesis in solid phase with the disappearance of a series of the most unstable peptides. The selection process with the formation of complementary peptides takes place in peptide synthesis under the thermal cyclic mode.

Trypsin-catalyzed Oligomerization of L-Lysine Esters

The oligomerization of L-lysine esters with a free α-amino group was done using trypsin as a catalyst in aqueous media, and some reaction parameters were examined.The pH-dependence of the reaction suggested that aminolysis by the substrate species having non-protonated α- and ε-amino groups was a dominant factor governing the reaction progress.At the beginning of the reaction lysine oligomers containing up to 8 residues were observed, but much of the dimer was accumulated during prolonged incubation due to secondary hydrolysis of highly polymerized products.The reaction yield depends on the ratio of enzyme and substrate; an overall reaction yield higher than 70 percent was attained after 2 hr of reaction when 1,000 mM of L-lysine ethyl ester was treated with 200 μM of trypsin at pH 10.0.The oligomerization was apparently enhanced by an addition of NaCl and by using the longer alkyl esters.