1571105-51-5

Basic information

• Product Name: C₆₀H₉₄N₁₂O₁₀
• Synonyms: C₆₀H₉₄N₁₂O₁₀
• CAS NO: 1571105-51-5
• Molecular Weight: 1143.48
• Mol File: 1571105-51-5.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: C₆₀H₉₄N₁₂O₁₀(CAS DataBase Reference)
• NIST Chemistry Reference: C₆₀H₉₄N₁₂O₁₀(1571105-51-5)
• EPA Substance Registry System: C₆₀H₉₄N₁₂O₁₀(1571105-51-5)

Safety Data

• Hazardous Substances Data: 1571105-51-5(Hazardous Substances Data)

Upstream product

• 15761-39-4 1-(tert-butoxycarbonyl)-L-proline 
• 13734-41-3 t-Boc-L-valine 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 3913-67-5 N-methylalanine 
• 2480-93-5 (R)-Nδ-benzyloxycarbonyl-Nα-(tert-butoxycarbonyl)-ornithine 
• 56564-52-4 N-methyl-D-phenylalanine 
• 18942-49-9 Boc-D-Phe-OH 

Relevant articles and documents

Dissociation of antimicrobial and hemolytic activities of gramicidin S through N-methylation modification

β-Sheet antimicrobial peptides (AMPs) are well recognized as promising candidates for the treatment of multidrug-resistant bacterial infections. To dissociate antimicrobial activity and hemolytic effect of b-sheet AMPs we hypothesize that N-methylation of the intramolecular hydrogen bond(s)-forming amides could improve their specificities for microbial cells over human erythrocytes. We utilized a model b-sheet antimicrobial peptide gramicidin S (GS) to study the N-methylation effects on the antimicrobial and hemolytic activities. We synthesized twelve N-methylated GS analogues by replacement of residues at the β-strand and β-turn regions with N-methyl amino acids and tested their antimicrobial and hemolytic activities. Our experiments showed that the HC50 values increased fivefold compared with that of GS when the internal hydrogen-bonded leucine residue was methylated. Neither hemolytic effect nor antimicrobial activity changed when proline alone was replaced with N-methylalanine in the b-turn region. However analogues containing N-methylleucine at β-strand and N-methylalanine at β-turn regions exhibited a fourfold increase in selectivity index compared to GS. We also examined the conformation of these N-methylated GS analogues using 1H NMR and circular dichroism (CD) spectroscopy in aqueous solution and visualized the backbone structures and residue orientations using molecular dynamics simulations. The results show that N-methylation of the internal hydrogen bond-forming amide affected the conformation backbone shape and side chain orientation of GS.