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Size-Dependent Cellular Uptake of RGD Peptides.


ABSTRACT: 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 PEG5000 peptide conjugate unveiled a selective internalization by M21 cells overexpressing ?v ?3 and no uptake in ?v -deficient M21L cells.

SUBMITTER: Kemker I 

PROVIDER: S-EPMC7064889 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature

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Size-Dependent Cellular Uptake of RGD Peptides.

Kemker Isabell I   Feiner Rebecca C RC   Müller Kristian M KM   Sewald Norbert N  

Chembiochem : a European journal of chemical biology 20191025 4


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 w  ...[more]

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