66438-39-9

Usage

Uses

Used in Pharmaceutical Industry:
BOC-LYS(2-CHLORO-Z)-OSU is used as a building block for the synthesis of synthetic peptides and peptide fragments. Its primary application is in the preparation of BDNF-mimetic dimeric dipeptide GSB-106, a potential neuroprotector drug. BOC-LYS(2-CHLORO-Z)-OSU holds promise in the treatment of neurodegenerative disorders and other conditions related to neuronal damage.
Used in Biotechnology Industry:
In the biotechnology sector, BOC-LYS(2-CHLORO-Z)-OSU serves as a key component in the development of novel bioactive peptides with potential applications in various therapeutic areas. Its versatility in peptide synthesis allows researchers to explore new avenues for drug discovery and the creation of targeted therapies for specific diseases.
Used in Research and Development:
BOC-LYS(2-CHLORO-Z)-OSU is also employed in research and development laboratories, where it is used to study the structure, function, and interactions of peptides. This knowledge can be applied to the design of new drugs and the understanding of peptide-based therapeutics, ultimately contributing to advancements in medicine and healthcare.

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 54613-99-9 Boc-(S)-Lys(2-Cl-Z)-OH 

Downstream Products

• 1385144-79-5 bis-(N-t-butyloxycarbonyl-Nε-(2-chlorobenzyloxycarbonyl)lysine)hexamethylenediamide 
• 128577-13-9 Boc-Lys(2Cl-Z)Glu(OH)-OPac 

Relevant academic research and scientific papers

Design and synthesis of dipeptide mimetics of the brain-derived neurotrophic factor

Low-molecular-weight mimetics of loops 1 and 4 of the brain-derived neurotrophic factor (BDNF) have been designed and synthesized. The compounds represent monomeric and dimeric amides of N-acyldipeptides. Their dipeptide fragments coincide in sequence with the central regions of beta-turns of the corresponding neurotrophin loops, and acyl groups are the bioesosteres of preceding amino acid residues. Hexa-or heptamethylenediamines were used as spacers to link the C-terminal regions of dipeptides in dimeric mimetics of BDNF. These compounds were synthesized by classical methods of peptide synthesis in solution and received the laboratory codes GSB-104 (HO-Suc-Ser-Lys-NH2), GSB-106 {[HO-Suc-Ser-Lys-NH-(CH2)3-]2}, GSB-207 (HO-Suc-Met-Ser-NH2), and GSB-214 ([HO-Suc-Met-Ser-NH-(CH2)7/2-]2). It was shown using immortalized hippocampal cells of the HT22 line under conditions of oxi-dative stress that the dimeric mimetics of both loops at concentrations of 10-5-10-8 M possess a neuropro-tective activity. The monomeric loop 1 mimetic GSB-207 in the same concentration range is inactive, and the monomeric loop 4 mimetic GSB-104 at a concentration of 10-7 impairs the survival of neurons. The find-ing that only dimeric mimetics possess the neuroprotective activity is consistent with the data indicating that BDNF is active in the homodimeric form. As opposed to the dimeric loop 1 mimetic GSB-214, the dimeric loop 4 mimetic GSB-106 exhibits the antidepressant activity typical for BDNF in the Porsolt test on rats at doses of 0.1 and 1 mg/kg injected intraperitoneally. This suggests that the antidepressant activity of BDNF is related to its 4th loop. We believe that the compounds obtained will be useful in studies of the mechanism of action of BDNF and may form the basis for the design of a novel group of drugs with antidepressant and neu-roprotective activities. Pleiades Publishing, Ltd., 2012.

Stabilized analogs of thymopentin. 1. 4,5-Ketomethylene pseudopeptides

The pentapeptide, thymopentin (Arg1-Lys2-Asp3-Val4-Tyr5) is known for its activity as an immunomodulating drug, but with limited half-life in plasma. In this first paper of a series of three studies, the synthesis of analogs stabilized at the peptide bond between the C-terminal amino acids via insertion of a ketomethylene moiety is described. N-Blocked pseudopeptides containing Val(k)Phe, Ala(k)Phe, and Val(k)Val units were prepared and attached to chloromethyl Merrifield resin via the carboxy terminal. Removal of the N-BOC group by trifluoroacetic acid was followed by sequential coupling with N-BOC dipeptides of aspartic acid to yield resin-bound N-BOC pseudotetrapeptides. Removal of N-BOC and coupling with N-BOC-r-N- tosylarginine followed by total cleavage of blocking groups and resin by HF afforded the target pseudopentapeptides. The analogs were found to compete favorably with thymopentin for binding to CEM cells, but binding was reduced by about 20-30% on average. All analogs showed significant enhancement of half-life versus thymopentin in mouse serum, but most showed only modest improvement in human serum. Insertion of proline or norleucine at position 2 in the chain caused a substantial increase in half-life (3-4-fold), while N- methylnorleucine conferred complete stability in the analogs.