158478-81-0

Usage

Uses

Used in Biochemistry and Molecular Biology:
Fmoc-HomoArg(Boc)2-OH is used as a protective group in peptide synthesis for the purpose of temporarily safeguarding reactive sites on the molecule during the synthesis process. This ensures the creation of precise, complex peptide chains, which are essential for studying protein behaviors and other biological phenomena.
Used in Pharmaceutical Industry:
Fmoc-HomoArg(Boc)2-OH is used as a key component in the development of new drugs and therapeutics. Its role in peptide synthesis allows for the creation of novel peptide-based compounds that can be tested for their potential medicinal properties, such as their ability to target specific diseases or conditions.
Used in Research and Development:
Fmoc-HomoArg(Boc)2-OH is used as a research tool in academic and industrial laboratories. Its application in peptide synthesis enables scientists to explore the structure and function of proteins, as well as to develop new methods for synthesizing complex peptide chains. This can lead to advancements in our understanding of biological processes and the development of new therapeutic strategies.

Upstream product

• 207857-15-6 1,3-di(tert-butyloxycarbonyl)-2-(trifluoromethylsulfonyl)guanidine 
• 139262-23-0 9-fluorenylmethoxycarbonyl-L-alanine hydrochloride 
• 71989-26-9 Fmoc-Lys(tert-butoxycarbonyl) 
• 332882-82-3 1,3-bis(t-butoxycarbonyl)guanidine 
• 24424-99-5 di-tert-butyl dicarbonate 
• 105047-45-8 Fmoc-Lys-OH 
• 152120-54-2 N,N'-bis( tert-butoxycarbonyl)-1H-pyrazole-1-carboxamidine 

Relevant academic research and scientific papers

Preparation method of eptifibatide key raw material L-higher arginine

The invention discloses a preparation method of an eptifibatide key raw material L-higher arginine, and belongs to the field of synthesis of medical intermediates. The preparation method comprises thefollowing steps: reacting 1,3-bis(tert-butyloxycarbonyl)guanidine with p-toluenesulfonyl chloride to obtain 1,3-bis-Boc-2-(p-toluenesulfonyl)guanidine, then reacting the 1,3-bis-Boc-2-(p-toluenesulfonyl)guanidine with N-fluorenylmethoxycarbonyl-N'-tert-butyloxycarbonyl-L-lysine Fmoc-hArg(Boc2)-OH, removing Boc protection, and feeding Pbf-Cl to obtain N-(9-fluorenylmethoxycarbonyl)-2,2,4,6,7-pentamethyl-2H-benzofuran-5-sulfonyl-L-arginine. According to the invention, a p-toluenesulfonyl polypeptide guanidinylating agent is adopted in the route, so that ultralow-temperature reaction and the useof trifluoromethanesulfonyl chloride or trifluoromethanesulfonic anhydride with high corrosivity are avoided, and a simple and efficient way is provided for the synthesis of the intermediate.

Attenuating HIV Tat/TAR-mediated protein expression by exploring the side chain length of positively charged residues

RNA is a drug target involved in diverse cellular functions and viral processes. Molecules that inhibit the HIV TAR RNA-Tat protein interaction may attenuate Tat/TAR-dependent protein expression and potentially serve as anti-HIV therapeutics. By incorpora

RNA virus-derived peptides with modified side chains

The present invention provides a RNA virus-derived peptides with modified side chains, wherein the side chains of the RNA virus-derived peptide are modified by altering the side-chain length or charges thereof such that the RNA virus-derived peptide has a high binding affinity for viral RNA and an high cellular uptake capability. The present invention also provides a composition for inhibiting RNA virus wherein the RNA virus-derived peptide can effectively inhibit viral self-replication and treat related diseases by its high affinity for viral RNA. A drug delivery carrier is also provided, wherein the RNA virus-derived peptides can carry desired drugs to the intracellular target due to its cellular uptake capability and thereby enhances the drug-delivery and treating efficiency.

Helix formation and capping energetics of arginine analogs with varying side chain length

Arginine (Arg) has been used for recognizing negatively charged biological molecules, cell penetration, and oligosaccharide mass signal enhancement. The versatility of Arg has inspired the need to develop Arg analogs and to research the structural effects of incorporating Arg analogs. Accordingly, we investigated the effect of Arg side chain length on helix formation by studying 12 Ala-based peptides containing the Arg analogs (S)-2-amino-6-guanidino- hexanoic acid (Agh), (S)-2-amino-4-guanidinobutyric acid (Agb), and (S)-2-amino-3-guanidinopropionic acid (Agp). Solid phase guanidinylation with orthogonal protection strategies was necessary to synthesize Agb- and Agp-containing peptides using Fmoc-based chemistry. The fraction helix for the peptides was determined by circular dichroism spectroscopy, and used to derive the statistical mechanical parameters and energetics for N-capping, C-capping, and helix propagation (propensity). All four Arg analogs were unfavorable for N-capping. The C-cap parameter followed the trend Agp Agh, highlighting the uniqueness of the Arg side chain length in helix formation. Molecular mechanics calculations and a survey on protein structures were consistent with the experimental results. Furthermore, calculations and survey both showed that the g- conformation for the χ1 dihedral was present for the first two residues at the N-terminus of helices, but not favored in the center or C-terminus of helices due to sterics. These results should serve as the foundation for developing Arg-related bioactive compounds and technologies.

Assessment of structurally diverse philanthotoxin analogues for inhibitory activity on ionotropic glutamate receptor subtypes: Discovery of nanomolar, nonselective, and use-dependent antagonists

An array of analogues of the wasp toxin philanthotoxin-433, in which the asymmetric polyamine moiety was exchanged for spermine and the headgroup replaced with a variety of structurally diverse moieties, was prepared using parallel solid-phase synthesis a

Total synthesis of the putative structure of lucentamycin A

A rapid and stereoselective enolate-Claisen rearrangement provides access to the 4-ethylidene-3-methylproline (Emp) subunit of lucentamycin A. Synthesis of the putative structure of the cytotoxic natural product suggests the need for structural revision.