188713-81-7

Basic information

• Product Name: L-Leucinamide, L-phenylalanyl-L-valyl-L-glutaminyl-L-tryptophyl-L-phenylalanyl-L-seryl-L-lys yl-L-phenylalanyl-L-leucylglycyl-L-arginyl-L-isoleucyl-
• CAS NO: 188713-81-7
• Molecular Formula: C83H122N20O15
• Molecular Weight: 1640.01
• Mol File: 188713-81-7.mol

Chemical Properties

• CAS DataBase Reference: L-Leucinamide, L-phenylalanyl-L-valyl-L-glutaminyl-L-tryptophyl-L-phenylalanyl-L-seryl-L-lys yl-L-phenylalanyl-L-leucylglycyl-L-arginyl-L-isoleucyl-(CAS DataBase Reference)
• NIST Chemistry Reference: L-Leucinamide, L-phenylalanyl-L-valyl-L-glutaminyl-L-tryptophyl-L-phenylalanyl-L-seryl-L-lys yl-L-phenylalanyl-L-leucylglycyl-L-arginyl-L-isoleucyl-(188713-81-7)
• EPA Substance Registry System: L-Leucinamide, L-phenylalanyl-L-valyl-L-glutaminyl-L-tryptophyl-L-phenylalanyl-L-seryl-L-lys yl-L-phenylalanyl-L-leucylglycyl-L-arginyl-L-isoleucyl-(188713-81-7)

Safety Data

• Hazardous Substances Data: 188713-81-7(Hazardous Substances Data)

Upstream product

• 29022-11-5 N-(fluoren-9-ylmethoxycarbonyl)glycine 
• 68858-20-8 Fmoc-Val-OH 
• 35661-60-0 Fmoc-Leu-OH 
• 35661-40-6 N-Fmoc L-Phe 
• 71989-33-8 Fmoc-Ser(tBu)-OH 
• 71989-23-6 Fmoc-Ile-OH 
• 71989-26-9 Fmoc-Lys(tert-butoxycarbonyl) 
• 132327-80-1 Fmoc-L-Gln(Trt)-OH 
• 143824-78-6 3-[(S)-2-carboxy-2-(9H-fluoren-9-ylmethoxycarbonylamino)ethyl]indole-1-carboxylic acid tert-butyl ester 
• 187618-60-6 Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine 

Relevant articles and documents

Photocontrolled compound release system using caged antimicrobial peptide

A novel photocontrolled compound release system using liposomes and a caged antimicrobial peptide was developed. The caged antimicrobial peptide was activated by UV irradiation, resulting in the formation of pores on the liposome surface to release the contained fluorophores. The compound release could be observed using fluorescence measurements and time-lapse fluorescence microscopy. UV irradiation resulted in a quick release of the inclusion compounds (within 1 min in most cases) under simulated physiological conditions. The proposed system is expected to be applicable in a wide range of fields from cell biology to clinical sciences.

Structure-activity relationship, conformational and biological studies of temporin l analogues

Temporins are naturally occurring peptides with promising features, which could lead to the development of new drugs. Temporin-1Tl (TL) is the strongest antimicrobial peptide, but it is toxic on human erythrocytes and this fact makes the design of synthetic analogues with a higher therapeutic index vital.We studied the structure-activity relationships of a library of TL derivatives focusing on the correlation between the α-helix content of the peptides, the nature of their cationic residues, and their antibacterial/antiyeast/ hemolytic activities. We found that the percentage of helicity of TL analogues is directly correlated to their hemolytic activity but not to their antimicrobial activity. In addition, we found that the nature of positively charged residues can affect the biological properties of TL without changing the peptide's helicity. It is noteworthy that a single amino acid substitution can prevent the antimicrobial activity of TL, making it a lytic peptide presumably due to its self-association. Last, we identified a novel analogue with properties that make it an attractive topic for future research.

The Outcomes of Decorated Prolines in the Discovery of Antimicrobial Peptides from Temporin-L

Previously, we identified a potent antimicrobial analogue of temporin L (TL), [Pro3]TL, in which glutamine at position 3 was substituted with proline. In this study, a series of analogues in which position 3 is substituted with non-natural proline derivatives, was investigated for correlations between the conformational properties of the compounds and their antibacterial, cytotoxic, and hemolytic activities. Non-natural proline analogues with substituents at position 4 of the pyrrolidine ring were considered. Structure–activity relationship (SAR) studies of these analogues were performed by means of antimicrobial and cytotoxicity assays along with circular dichroism (CD) and NMR spectroscopic analyses for selected compounds. The most promising peptides were additionally evaluated for their activity against some representative veterinary microbial strains to compare with those from human strains. We identified novel analogues with interesting properties that make them attractive lead compounds.