Conjugation of spermine enhances cellular uptake of the stapled peptide-based inhibitors of p53-Mdm2 interaction

Avinash Muppidi; Xiaolong Li; Jiandong Chen; Qing Lin

doi:10.1016/j.bmcl.2011.10.009

Conjugation of spermine enhances cellular uptake of the stapled peptide-based inhibitors of p53-Mdm2 interaction

Avinash Muppidi
, Xiaolong Li
, Jiandong Chen
, Qing Lin

Chemistry

SUNY Buffalo
Moffitt Cancer Center

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

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.

Original language	English
Pages (from-to)	7412-7415
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	21
Issue number	24
DOIs	https://doi.org/10.1016/j.bmcl.2011.10.009
State	Published - Dec 15 2011

Keywords

Cellular uptake
Helical structure
Peptides
Protein-protein interaction
Spermine

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10.1016/j.bmcl.2011.10.009

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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.",

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AU - Muppidi, Avinash

AU - Li, Xiaolong

AU - Chen, Jiandong

AU - Lin, Qing

PY - 2011/12/15

Y1 - 2011/12/15

N2 - 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.

AB - 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.

KW - Cellular uptake

KW - Helical structure

KW - Peptides

KW - Protein-protein interaction

KW - Spermine

UR - https://www.scopus.com/pages/publications/81255198354

U2 - 10.1016/j.bmcl.2011.10.009

DO - 10.1016/j.bmcl.2011.10.009

M3 - Article

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AN - SCOPUS:81255198354

SN - 0960-894X

VL - 21

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JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 24

ER -

Conjugation of spermine enhances cellular uptake of the stapled peptide-based inhibitors of p53-Mdm2 interaction

Abstract

Keywords

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