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• W2034244987 abstract "Peptide-mediated targeted delivery offers an attractive strategy for selective delivery of cytotoxic drugs to cancer cells. In this work, we have investigated the mechanism of internalization of cIBR peptide [cyclo(1,12)PenPRGGSVLVTGC] that is conjugated with fluorescein isothiocyanate (FITC) and doxorubicin (DOX) to give FITC–cIBR and DOX–cIBR conjugates, respectively. Internalization mechanisms of FITC–cIBR and DOX–cIBR were studied in LFA-1-expressing cells (HL-60) and LFA-1-deficient cells (HUVEC) under the following conditions: (a) at two different temperatures (4 and 37 °C), (b) in the presence of ATP-depleting agents (sodium azide and 2-deoxy-d-glucose), and (c) in the presence of a microtubule-disrupting agent (nocodazole). At 37 °C, FITC–cIBR was internalized by HL-60 cells and located in the endosomes; however, it was not internalized by LFA-1-deficient HUVEC. Incubation of FITC–cIBR at 4 °C or in the presence of nocodazole inhibited its endocytosis in HL-60 cells. The ATP inhibitors inhibited the internalization of FITC–cIBR but maintained its binding to cell surface receptors. In contrast, DOX–cIBR was diffusely distributed in the cytoplasm of LFA-1-expressing HL-60 cells following incubation at 37 °C. No inhibitory processes could block the entry or change the distribution pattern of DOX–cIBR into HL-60 cells, suggesting that DOX–cIBR uptake was not mediated by receptors such as LFA-1. DOX–cIBR was still found inside HUVEC, but with a distribution pattern somewhat different from that in HL-60 cells. The major entry mechanism of DOX–cIBR could be via passive diffusion because DOX–cIBR has an octanol/water distribution coefficient (Log D) of 1.15. Thus, DOX–cIBR is more lipophilic than FITC–cIBR with a Log D of 0.57. Therefore, the change in the hydrophobicity of the conjugate may alter the mechanism of entry of DOX–cIBR compared to that of FITC–cIBR. This study suggests that alteration of the physicochemical properties of drug–peptide conjugates can change the mode of uptake from receptor-mediated uptake to passive diffusion." @default.
• W2034244987 created "2016-06-24" @default.
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• W2034244987 date "2007-08-07" @default.
• W2034244987 modified "2023-10-14" @default.
• W2034244987 title "Mechanism of Internalization of an ICAM-1-Derived Peptide by Human Leukemic Cell Line HL-60: Influence of Physicochemical Properties on Targeted Drug Delivery" @default.
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• W2034244987 doi "https://doi.org/10.1021/mp0700458" @default.
• W2034244987 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17680719" @default.
• W2034244987 hasPublicationYear "2007" @default.
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