141743-14-8

Basic information

• Product Name: Glycine, N-[(9H-fluoren-9-ylmethoxy)carbonyl]-N-(2-methylpropyl)-
• Synonyms: Fmoc-NLeu-OH
• CAS NO: 141743-14-8
• Molecular Formula: C21H23NO4
• Molecular Weight: 353.418
• Mol File: 141743-14-8.mol
• Article Data: 4

Chemical Properties

• Boiling Point: 533.1±29.0 °C(Predicted)
• Density: 1?+-.0.06 g/cm3(Predicted)
• CAS DataBase Reference: Glycine, N-[(9H-fluoren-9-ylmethoxy)carbonyl]-N-(2-methylpropyl)-(CAS DataBase Reference)
• NIST Chemistry Reference: Glycine, N-[(9H-fluoren-9-ylmethoxy)carbonyl]-N-(2-methylpropyl)-(141743-14-8)
• EPA Substance Registry System: Glycine, N-[(9H-fluoren-9-ylmethoxy)carbonyl]-N-(2-methylpropyl)-(141743-14-8)

Safety Data

• Hazardous Substances Data: 141743-14-8(Hazardous Substances Data)

Usage

General Description

"Glycine, N-[(9H-fluoren-9-ylmethoxy)carbonyl]-N-(2-methylpropyl)-" is a complex chemical compound associated with organic chemistry. It combines elements from the Glycine amino acid and fluorene, a polycyclic aromatic hydrocarbon. The compound is characterized by an N-(9H-fluoren-9-ylmethoxy)carbonyl group, which represents a fluorenylmethyloxycarbonyl (Fmoc) protecting group utilized in peptide synthesis. It is also notable for the presence of a 2-methylpropyl or isobutyl group. Glycine, N-[(9H-fluoren-9-ylmethoxy)carbonyl]-N-(2-methylpropyl)- is typically used in research areas and in the production of synthetic peptides and proteins.

Upstream product

• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 3182-87-4 N-isobutylglycine ethyl ester 
• 3182-85-2 N-Isobutylglycin 

Downstream Products

• 919524-67-7 2-{(1E)-2-aza-2-[(5-{N-[5-(N-{2-[(2-methylropyl)amino]-acetylamino}-carbamoyl)pentyl]carbamoyl}(2-pyridyl))amino]vinyl}benzenesulfonic acid 

Relevant articles and documents

Effect of double replacement of L-Pro, D-Pro, D-Leu or Nleu in hydrophobic face of amphipathic α-helical model antimicrobial peptide on structure, cell selectivity and mechanism of action

In order to investigate the effects of the double replacement of L-Pro, D-Pro, D-Leu or Nleu (the peptoid residue for Leu) in the hydrophobic face (positions 9 and 13) of amphipathic α-helical non-cell-selective antimicrobial peptide L8K9W1 on the structure, cell selectivity and mechanism of action, we synthesized a series of L8K9W1analogs with double replacement of L-Pro, D-Pro, D-Leu or Nleu in the hydrophobic face of L8K9W1. In this study, we have confirmed that the double replacement of L-Pro, D-Pro, or Nleu in the hydrophobic face of L8K9W1 let to a great increase in the selectivity toward bacterial cells and a complete destruction of α-helical structure. Interestingly, L8K9W1-L-Pro, L8K9W1-D-Pro and L8K9W1-Nleu preferentially interacted with negatively charged phospholipids, but unlike L8K9W1 and L8K9W1-D-Leu, they did not disrupt the integrity of lipid bilayers and depolarize the bacterial cytoplasmic membrane. These results suggested that the mode of action of L8K9W1-L-Pro, L8K9W1-D-Pro and L8K9W1-Nleu involves the intracellular target other than the bacterial membrane. In particular, L8K9W1-L-Pro, L8K9W1-D-Pro and L8K9W1-Nleu had powerful antimicrobial activity (MIC range, 1 to 4 μM) against methicillin-resistant Staphylococcus aureus (MRSA) and multidrug-resistant Pseudomonas aeruginosa (MDRPA). Taken together, our results suggested that L8K9W1-L-Pro, L8K9W1-D-Pro and L8K9W1-Nleu with great cell selectivity may be promising candidates for novel therapeutic agents, complementing conventional antibiotic therapies to combat pathogenic microorganisms.

HYDRAZIDE CONJUGATES AS IMAGING AGENTS

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