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- W2012000552 abstract "Following the successful approval of the first HIV-1 fusion inhibitor, enfuvirtide (formerly T-20), T-1249 was developed to be one of the next generation drug of this type. Previous studies, based on tryptophan intrinsic fluorescence, showed that these peptides interact with membrane model systems (large unilamellar vesicles) of different lipid compositions. Studies with human blood cell membranes were necessary to further establish the role of membranes on these peptides mode of action. An experimental strategy was applied taking into account the membrane dipole potential as measured by the potential sensitive fluorescent probe di-8-ANEPPS. Successful labelling was performed with erythrocytes and peripheral blood mononuclear cells (PBMC) isolated from human blood samples.For erythrocytes, membrane bound di-8-ANEPPS excitation spectra were blue shifted, indicating a decrease in the dipole potential due to peptide-membrane interactions. Accordingly, a decrease in the probe fluorescence excitation ratio (a measure of the spectral shift) dependent of peptide concentration was observed. The quantitative analysis of these variations indicated that T-1249 had the higher affinity towards erythrocyte membrane. This is in agreement with the previously known adsorption of this peptide on cholesterol-rich membrane domains.Preliminary results show that the behaviour is similar in the case of PBMC, with a decrease in dipole potential that is more pronounced for T-1249. As there is strong suggestion that HIV also associates with erythrocytes in vivo, the peptide concentration effect of the erythrocytes and lymphocyte membranes can correlate with the stronger efficacy of T-1249." @default.
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- W2012000552 date "2009-02-01" @default.
- W2012000552 modified "2023-09-28" @default.
- W2012000552 title "Human Erythrocytes And Mononuclear Leukocytes Are Capable Of Concentrating HIV-1 Fusion Inhibitor Peptides In Their Membranes" @default.
- W2012000552 doi "https://doi.org/10.1016/j.bpj.2008.12.715" @default.
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