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Size‐Dependent Cellular Uptake of RGD Peptides
Author(s) -
Kemker Isabell,
Feiner Rebecca C.,
Müller Kristian M.,
Sewald Norbert
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900512
Subject(s) - peptide , endocytosis , internalization , linker , chemistry , conjugate , derivatization , biophysics , lysine , flow cytometry , click chemistry , ethylene glycol , peptide synthesis , biochemistry , combinatorial chemistry , cell , amino acid , microbiology and biotechnology , biology , chromatography , mathematical analysis , high performance liquid chromatography , mathematics , organic chemistry , computer science , operating system
Monomeric RGD peptides show unspecific fluid‐phase uptake in cells, whereas multimeric RGD peptides are thought to be internalized by integrin‐mediated endocytosis. However, a potential correlation between uptake mechanism and molecular mass has been neglected so far. A dual derivatization of peptide c (RGDw(7Br)K) was performed to investigate this. A fluorescent probe was installed by chemoselective Suzuki–Miyaura cross‐coupling of the 7‐bromotryptophan and a poly(ethylene glycol) (PEG) linker was attached to the lysine residue. Flow cytometry and live cell imaging confirmed unspecific uptake of the small, non‐PEGylated peptide, whereas the PEG 5000 peptide conjugate unveiled a selective internalization by M21 cells overexpressing α v β 3 and no uptake in α v ‐deficient M21L cells.