Fluoro‐modified chemotactic peptides: fmlf analogues

Abstract

A small library of peptide analogues of the chemotactic tripeptide For-Met-Leu-Phe-NH2 modified by substitution of Leu at position 2 by three different fluorinated amino acids varying in content of fluorine, length of the fluorinated side chain, and alkylation degree at the alpha-carbon atom was synthesized. The influence of the fluorine substitution on the biological activity was investigated by measuring the oxidative activity of neutrophils using a luminol-dependent chemiluminescence assay.

Fluorine in Peptide Design and Protein Engineering

“…A small library of the chemoattractant For-Met-Leu-Phe-NH 2 (fMLF) has been synthesized by substituting Leu in position 2 with different fluorinated amino acids that vary in the content of fluorine, the length of the fluorinated side chain, and the degree of alkylation at the α-carbon atom. [147] Chemoattractants, like fMLF that is produced by Escherichia coli, [148,149] are involved in the activation process of antibacterial chemotaxis, the directed movement of cells along a chemical gradient. [150] The response to infection starts with the movement of neutrophils toward the bacteria.…”

Enantioselective synthesis of (2R, 3S)‐ and (2S, 3R)‐4,4,4‐trifluoro‐N‐Fmoc‐O‐tert‐butyl‐threonine and their racemization‐free incorporation into oligopeptides via solid‐phase synthesis

“…The residue was purified by column chromatography on silica gel (ethyl acetate : methanol = 9 : 1) to give Fmoc-1a(tBu)-OH as a white solid (4.7 g, 91%). Fmoc-1a(tBu)-OH was recrystallized from hexanes and CH 2 Cl 2 to achieve higher purity: [α] 7,157.4,144.1,144.0,141.3,127.6,127.0,125.3,125.1,125.0 (q,J = 283.2 Hz),119.7,76.9,70.9 (q,J = 28.4 Hz),67.1,57.6,29.7,27. (2R, 3S)-Benzoic acid 4,4,4-trifluoro-2,3-bis-((R)-3,3,3-trifluoro-2-methoxy-2 5,165.3,139.3,136.7,133.7,131.0,130.4,130.2,129.8,128.8,128.6,128.5,127.4,127.3,123.0 (q,J = 288.7 Hz),122.8 (q,J = 287.9 Hz), 120.0 (q, J = 281.7 Hz), 85.1 (q, J = 29.1 Hz), 68.5 (q,J = 32.9 Hz),68.1,61.2,55.5,55.4,29.7;MS (CI) 61.6, 59.4, 55.1, 51.0, 48.9, 43.0, 42.7, 28.5, 27.1, 26.6, 19.9, 19.4 68.3,59.5,58.0,54.3,51.9,48.9,…”

“…7 Furthermore, incorporation of fluorinated amino acids makes it possible to investigate the conformation and metabolism of host peptides or proteins by 19 F NMR. 8 The multi-faceted impact of fluorinated amino acids on peptides and proteins was discussed in a recent review.…”

“…9 From a pharmaceutical chemistry standpoint, fluorinated amino acids can be used as pharmacokinetic modulators (via prolonged in vivo half-life, t ½ ) and reporters (via 19 F NMR) for peptide-based pharmaceuticals. 10 Several methods have been developed for site-specific incorporation of fluorinated amino acids into peptides or proteins, including both solid-1, 2, 3 and solution- 7,11 phase chemical synthesis, protease-catalyzed synthesis 12 and in vivo bio-synthesis. 13 Among these methods, solid-phase peptide synthesis (SPPS) is still the most commonly used one due to its ease of operation.…”

Characterization of acrylic copolymer latex modified by fluorine, silicon, and epoxy resin

“…The structure of alternating carbon / hydrogen bonds with carbon / fluorine bonds, in combination with the high bond strength of carbon-fluorine atoms (486 kJ/mol) in fluorinated polymers, provides chemical inertness that enables the formulation of fluorinated polymers to resist environmental degradation (i.e., to solvents, chemicals, acid and base, oxidation, airborne pollutants) and the ultra low surface energy reduces dirt retention [5][6][7]. Due to the unique characteristics, fluorinated polymers have been widely studied in recent years.…”