1433875-42-3Relevant academic research and scientific papers
Fluorescent peptides labeled with environment-sensitive 7-aminocoumarins and their interactions with lipid bilayer membranes and living cells
Murase, Tokiko,Yoshihara, Toshitada,Yamada, Keiichi,Tobita, Seiji
supporting information, p. 510 - 519 (2013/06/04)
The photophysical properties of protected nonnatural amino acids BocL- Dap(7DEAC)OMe (7DEAC: 7-diethylaminocoumarin) and BocL- Dap(C343)OMe (C343: coumarin 343) were investigated to evaluate the suitability of these amino acids as fluorescent units in peptide-based fluorescent biosensors. The absorption and fluorescence spectra of BocL- Dap(7DEAC)OMe and BocL- Dap(C343)OMe exhibited significant red shifts with increasing solvent polarity. The fluorescence quantum yield and lifetime of BocL- Dap(7DEAC)OMe solutions decreased remarkably with increasing solvent polarity, whereas those of BocL- Dap(C343)OMe were slightly affected by the solvent polarity. Fluorescent peptides HDap( 7DEAC)LLAOMe (1), HDap( 7DEAC)KLAOMe (2), and HDap( 7DEAC)ELAOMe (3) labeled with environment-sensitive 7DEAC were synthesized to examine the interactions of these labeled peptides with lipid membranes and living cells. Neutral 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and anionic 1,2-dimyristoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (DMPG) liposomes were used to investigate peptidemembrane interactions. Hydrophobic peptide 1 exhibited high affinities to both DMPC and DMPC/DMPG mixed membranes. Of the three peptides, cationic peptide 2 exhibited the strongest affinity to DMPC/DMPG membranes, whereas anionic peptide 3 showed a much lower affinity to DMPC/DMPG membranes. These results could be interpreted based on hydrophobic and electrostatic interactions between the peptides and membranes. Peptide 1 was efficiently internalized into HeLa cells, whereas peptides 2 and 3 showed a much lower intracellular delivery.
