37574-72-4

Upstream product

• 74-79-3 L-arginine 
• 100-46-9 benzylamine 
• 751452-36-5 Boc-L-Arg-NHBzl 
• 13726-76-6 t-butyloxycarbonyl-L-arginine 

Downstream Products

• 1184963-09-4 N-α-Boc-L-His-L-Arg-NHBzl 
• 1185192-55-5 L-His-L-Arg-NHBzl 
• 1537176-74-1 Boc-His(phenyl)-Arg-NHBzl 
• 1613201-39-0 His(phenyl)-Arg-NHBzl 
• 1537176-76-3 Boc-His(4-methylphenyl)-Arg-NHBzl 
• 1613201-40-3 His(4-methylphenyl)-Arg-NHBzl 
• 1537176-77-4 Boc-His(4-methoxyphenyl)-Arg-NHBzl 
• 1613201-41-4 His(4-methoxyphenyl)-Arg-NHBzl 
• 1537176-78-5 Boc-His(4-t-butylphenyl)-Arg-NHBzl 
• 1613201-42-5 His(4-t-butylphenyl)-Arg-NHBzl 
• 1537176-79-6 Boc-His(biphenyl)-Arg-NHBzl 
• 1613201-43-6 His(biphenyl)-Arg-NHBzl 
• 1613201-44-7 His(naphthyl)-Arg-NHBzl 
• 1613201-38-9 Boc-His(naphthyl)-Arg-NHBzl 

Relevant academic research and scientific papers

Modified histidine containing amphipathic ultrashort antifungal peptide, His[2-p-(n-butyl)phenyl]-Trp-Arg-OMe exhibits potent anticryptococcal activity

In pursuit of ultrashort peptide-based antifungals, a new structural class, His(2-aryl)-Trp-Arg is reported. Structural changes were investigated on His-Trp-Arg scaffold to demonstrate the impact of charge and lipophilic character on the biological activity. The presence and size of the aryl moiety on imidazole of histidine modulated overall amphiphilic character, and biological activity. Peptides exhibited IC50 of 0.37–9.66 μg/mL against C. neoformans. Peptide 14f [His(2-p-(n-butyl)phenyl)-Trp-Arg-OMe] exhibited two-fold potency (IC50 = 0.37 μg/mL, MIC = 0.63 μg/mL) related to amphotericin B, without any cytotoxic effects up to 10 μg/mL. Peptide 14f act by nuclear fragmentation, membranes permeabilization, disruption and pore formations in the microbial cells as determined by the mechanistic studies employing Trp-quenching, CLSM, SEM, and HR-TEM. The amalgamation of short sequence, presence of appropriate aryl group on L-histidine, potent anticryptococcal activity, no cytotoxicity, and detailed mechanistic studies directed to the identification of 14f as a new antifungal structural lead.

Unprecedented 1,1′-carbonyldiimidazole-mediated amidation of unprotected α-amino acids in water

The first amidation reaction of unprotected α-amino acids in water under neutral conditions with various aliphatic, aromatic and heteroaromatic amines in the presence of coupling reagent 1,1′-carbonyldiimidazole at ambient temperature is described. Georg Thieme Verlag Stuttgart.

Alkylated histidine based short cationic antifungal peptides: Synthesis, biological evaluation and mechanistic investigations

Current clinically used antifungal agents suffer from several drawbacks that have urgently necessitated the development of new antifungal agents with unusual mechanisms of action. In this context, antifungal peptides (AFPs) open up new perspectives in drug design by providing an entire range of highly selective and nontoxic pharmaceuticals. Here, we report the development of novel short AFPs with the synthesis of two series of tripeptide based compounds named as His(2-alkyl)-Arg-Lys (series I) and His(2-alkyl)-Arg-Arg (series II). The series II peptides were found to be selectively active against Cryptococcus neoformans whereas some peptides displayed encouraging activities against other fungal strains such as Candida albicans, Candida kyfer, Aspergillus Niger and Neurospora crassa. The cytotoxic experiments were performed on active compounds using Hek-293 and HeLa cells which exhibited negligible cytotoxic effect up to the highest test concentration. Further, the most potent peptide was subjected to mechanistic studies using TEM analysis. Two sets of SUVs mimicking microbial membrane and mammalian membrane were treated with the most potent peptide. The results of this study were found to be perfectly in corroboration with the antifungal activity in relation to the differences between microbial and mammalian cell membrane composition, thereby, indicating that the reported peptides may also be less susceptible to the common mechanisms of drug resistance.

Synthesis and antimicrobial activities of His(2-aryl)-Arg and Trp-His(2-aryl) classes of dipeptidomimetics

In this communication, we report the design, synthesis and in vitro antimicrobial activity of ultra short peptidomimetics. Besides producing promising antibacterial activities against Staphylococcus aureus and methicillin-resistant S. aureus (MRSA), the dipeptidomimetics exhibited high antifungal activity against C. neoformans with IC50 values in the range of 0.16-19 μg mL-1. The most potent analogs exhibited 4-fold higher activity than the currently used drug amphotericin B, with no apparent cytotoxicity in a panel of mammalian cell lines. This journal is the Partner Organisations 2014.

Albumin binding of short cationic antimicrobial micropeptides and its influence on the in vitro bactericidal effect

The interactions between a range of small cationic antibacterial tripeptides and bovine and human serum albumin in a buffered aqueous solution at 25°C have been studied using isothermal titration calorimetry. Results from the binding study indicate a sing