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Effect of modification of the physicochemical properties of ICAM-1-derived peptides on internalization and intracellular distribution in the human leukemic cell line HL-60. | LitMetric

The objective of this work is to test the hypothesis that increasing the hydrophilicity of DOX-peptide conjugates may modify their entry mechanisms into HL-60 cells from passive diffusion to receptor-mediated uptake. To test this hypothesis, the entry mechanisms and the intracellular disposition of DOX-cIBR7, DOX-PEGcIBR7, FITC-cIBR, and FITC-cIBR7 were evaluated in HL-60 cells. To increase the hydrophilicity of the peptide, the cIBR peptide (cyclo(1,12)Pen-PRGGSVLVTGC) was modified to cIBR7 peptide (cyclo(1,8)CPRGGSVC) by removing the hydrophobic residues at the C-terminus. DOX-cIBR7 conjugate, which has higher hydrophilicity than DOX-cIBR, was synthesized. Second, a hydrophilic linker (11-amino-3,6,9-trioxaundecanate linker) was incorporated between DOX and cIBR7 to generate DOX-PEGcIBR7 with higher hydrophilicity than DOX-cIBR7. As controls, FITC-cIBR and FITC-cIBR7 were used to check for any endocytic uptake process of the peptide. As previously found with DOX-cIBR, DOX-cIBR7, and DOX-PEGcIBR7, conjugates enter the cells via passive diffusion and not via the energy-dependent endocytic process. This result suggests that an increase in hydrophilicity does not influence the entry mechanism of the DOX-peptide conjugates. In contrast to the DOX-cIBR7 conjugate, the FITC-cIBR7 conjugate showed energy-dependent cellular entry into the cells and followed an endocytic pathway similar to that for dextran. Finally, the entry of DOX-cIBR7 and DOX-PEGcIBR into the cell cytosol was shown to be due to the properties of DOX and not to those of the peptide.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2683983PMC
http://dx.doi.org/10.1021/mp800120tDOI Listing

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