206183-06-4

Usage

Uses

Used in Pharmaceutical Industry:
Fmoc-L-Norarginine(Boc)2-OH, (S)-N-alpha-(9-Fluorenylmethyloxycarbonyl)-N,N-bis-t-butyloxycarbonyl-2-amino-4-guanidino-butyric acid is used as a building block for the synthesis of peptides containing Arginine and its two homologs. This application is crucial in the development of various therapeutic peptides with potential applications in treating a range of medical conditions.
Used in Biochemical Research:
In the field of biochemical research, Fmoc-L-Norarginine(Boc)2-OH, (S)-N-alpha-(9-Fluorenylmethyloxycarbonyl)-N,N-bis-t-butyloxycarbonyl-2-amino-4-guanidino-butyric acid is used as a precursor in the preparation of Arylalkanoylaminoacetamides. These compounds are of interest as potential inhibitors of blood coagulation factor Xa, which plays a key role in the coagulation cascade. Inhibiting factor Xa can be beneficial in the development of anticoagulant drugs for the treatment of conditions such as deep vein thrombosis, pulmonary embolism, and other clot-related disorders.
Used in Chemical Synthesis:
Fmoc-L-Norarginine(Boc)2-OH, (S)-N-alpha-(9-Fluorenylmethyloxycarbonyl)-N,N-bis-t-butyloxycarbonyl-2-amino-4-guanidino-butyric acid is also utilized in chemical synthesis as an intermediate for the production of various complex organic molecules. Its unique structure and functional groups make it a valuable component in the synthesis of a wide range of compounds with diverse applications in the pharmaceutical, agrochemical, and materials science industries.

Upstream product

• 207857-15-6 1,3-di(tert-butyloxycarbonyl)-2-(trifluoromethylsulfonyl)guanidine 

Relevant academic research and scientific papers

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.