title: Conjugation of spermine enhances cellular uptake of the stapled peptide-based inhibitors of p53-Mdm2 interaction.
abstract: We report the first synthesis of the C-terminally spermine-conjugated stapled peptide-based inhibitors of the p53-Mdm2 interaction. Subsequent biological, biophysical and cellular uptake assays with the spermine-conjugated stapled peptides revealed that spermine conjugation minimally affects biological activity while significantly increases peptide helicity and cellular uptake without apparent cytotoxicity.
authors: Department of Chemistry, State University of New York at Buffalo, Buffalo, NY 14260, USA.
authors: Avinash
authors: A
authors: Muppidi
authors: Xiaolong
authors: X
authors: Li
authors: Jiandong
authors: J
authors: Chen
authors: Qing
authors: Q
authors: Lin
mesh_terms: D000595:Amino Acid Sequence; D002470:Cell Survival / Q000187:drug effects; D002477:Cells / Q000187:drug effects; D002942:Circular Dichroism; D019793:Fluorescein / Q000737:chemistry; D006367:HeLa Cells; D006801:Humans; D008856:Microscopy, Fluorescence; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D051736:Proto-Oncogene Proteins c-mdm2 / Q000037:antagonists & inhibitors* / Q000378:metabolism; D013096:Spermine / Q000737:chemistry*; D016159:Tumor Suppressor Protein p53 / Q000037:antagonists & inhibitors* / Q000378:metabolism
chemical_list: D010455:Peptides; D016159:Tumor Suppressor Protein p53; D013096:Spermine; C497206:MDM2 protein, human; D051736:Proto-Oncogene Proteins c-mdm2; D019793:Fluorescein