https://www.selleckchem.com/products/LBH-589.html In a previous work, we defined a novel HIV-1 fusion inhibitor peptide (E1P47) with a broad spectrum of activity against viruses from different clades, subtypes, and tropisms. With the aim to enhance its efficacy, in the present work we address the design and synthesis of several peptide amphiphiles (PAs) based on the E1P47 peptide sequence to target the lipid rafts of the cell membrane where the cell-cell fusion process takes place. We report the synthesis of novel PAs having a hydrophobic moiety covalently attached to the peptide sequence through a hydrophilic spacer of polyethylene glycol. Characterization of self-assembly in condensed phase and aqueous solution as well as their interaction with model membranes was analyzed by several biophysical methods. Our results demonstrated that the length of the spacer of polyethylene glycol, the position of the peptide conjugation as well as the type of the hydrophobic residue determine the antiviral activity of the construct. Peptide amphiphiles with one alkyl tail either in C-terminus (C-PAmonoalkyl) or in N-terminus (N-PAmonoalkyl) showed the highest anti-HIV-1 activities in the cellular model of TZM-bl cells or in a preclinical model of the human mucosal tissue explants.Nanoscale zero-valent iron (nZVI) has become one of the most used engineered nanoparticles for soil remediation. However, isolating nZVI particles from a complex soil matrix for their accurate particle characterizations and transport distance measurements is still challenging. Here, this study established a new analysis approach combining ultrasound-assisted solvent extraction, magnetic separation, and single particle inductively coupled plasma mass spectrometry (SP-ICP-MS) analysis to isolate nZVI particles from soils and quantify their concentration and size. The interference from natural Fe-containing substances on nZVI analysis could be efficiently minimized by magnetic separation and dilution. After