313232-63-2

Basic information

• Product Name: Fmoc-Alg(Boc)2-OH
• Synonyms: Fmoc-Alg(Boc)2-OH;FMoc-Agp(Boc)2-OH;(3S)-3-Carboxy-6-[[(1,1-dimethylethoxy)carbonyl]amino]-10,10-dimethyl-8-oxo-9-oxa-2,5,7-triazaundec-5-enoic acid 1-(9H-fluoren-9-ylmethyl) ester;Fmoc-L-Alg(Boc)2-OH
• CAS NO: 313232-63-2
• Molecular Formula: C29H36N4O8
• Molecular Weight: 568.61814
• Product Categories: amino acids
• Mol File: 313232-63-2.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• Density: 1.28±0.1 g/cm3(Predicted)
• Storage Temp.: Store at -15°C to -25°C.
• PKA: 3.31±0.10(Predicted)
• CAS DataBase Reference: Fmoc-Alg(Boc)2-OH(CAS DataBase Reference)
• NIST Chemistry Reference: Fmoc-Alg(Boc)2-OH(313232-63-2)
• EPA Substance Registry System: Fmoc-Alg(Boc)2-OH(313232-63-2)

Safety Data

• Hazardous Substances Data: 313232-63-2(Hazardous Substances Data)

Usage

General Description

Fmoc-Alg(Boc)2-OH is a chemical compound that consists of an N-terminal Fmoc group, two Boc-protected amino acids, and a carboxylic acid group. The Fmoc group serves as a protective group for the N-terminal amine, while the Boc groups protect the two amino acids. Fmoc-Alg(Boc)2-OH is often used in solid-phase peptide synthesis to build peptides in a stepwise fashion. The Fmoc-Alg(Boc)2-OH compound allows for the controlled addition of amino acids to the growing peptide chain and can be deprotected and cleaved from the solid support after the peptide synthesis is complete.

Upstream product

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

Relevant articles and documents

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.