Fluorinated amino acids and peptides. Synthesis of 3,3-difluoro-2-amino acids, peptides and cyclodipeptides incorporating 3,3-difluoro-2-aminobutyric acid or 3,3-difluorophenylalanine residues in their structures

Ayi, A.I.; Martos-Alcaniz, M.-L.; Condom, Roger; Frogier, P. R. T.; Guedj, R.

doi:10.1016/s0022-1139(00)81249-x

Cited by 3 publications

(1 citation statement)

References 29 publications

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“…A slight modification to the original procedure, adding PPh 3 first and leaving to stir for 5 h before adding water, increased the yield to 93%. Fmoc protection to give 18 was followed by removal of the tert -butyl group to give the desired lipophilic amino acid Fmoc-Laa 4 in 46% overall yield from 11 .…”

Section: Resultsmentioning

confidence: 99%

Targeting Lipopolyplexes Using Bifunctional Peptides Incorporating Hydrophobic Spacer Amino Acids: Synthesis, Transfection, and Biophysical Studies

et al. 2007

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We have developed efficient synthetic routes to two hydrophobic amino acids, suitably protected for solid-phase peptide synthesis, and have successfully synthesized peptides containing these or other hydrophobic amino acids as spacers between a Lys16 moiety and an integrin-targeting motif. These peptides have in turn been used to formulate a range of lipopolyplex vectors with Lipofectin and plasmid DNA. The transfection efficiencies of these vectors and their aggregation behavior in buffers and in serum have been studied. We have shown that vectors containing peptides incorporating long linkers that are entirely hydrophobic are less efficient transfection agents. However, linkers of equivalent length that are in part hydrophobic show improved transfection properties, which is probably due to the improved accessibility of the integrin-binding motif.

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Section: Resultsmentioning

confidence: 99%