Cell-Penetrating cis-γ-Amino-l-Proline-Derived Peptides

The synthesis of cis-γ-amino-l-proline oligomers functionalized at the proline α-amine with several groups that mimic the side chains of natural amino acids, including alanine, leucine, and phenylalanine, is herein described. These γ-peptides enter into different cell lines (COS-1 and HeLa) via an e...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2005-07, Vol.127 (26), p.9459-9468
Main Authors: Farrera-Sinfreu, Josep, Giralt, Ernest, Castel, Susanna, Albericio, Fernando, Royo, Miriam
Format: Article
Language:English
Subjects:
Alanine - chemistry
Aminoacid polymers
Animals
Applied sciences
Cell Membrane - metabolism
Cercopithecus aethiops
Endocytosis
Exact sciences and technology
Flow Cytometry
Gene Products, tat - chemistry
Gene Products, tat - metabolism
Gene Products, tat - toxicity
HeLa Cells
Humans
Leucine - chemistry
Microscopy, Confocal
Microscopy, Fluorescence
Peptide Hydrolases - metabolism
Peptides - chemical synthesis
Peptides - metabolism
Phenylalanine - chemistry
Physicochemistry of polymers
Proline - analogs & derivatives
Proline - chemistry
Synthetic biopolymers
Temperature
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Summary:The synthesis of cis-γ-amino-l-proline oligomers functionalized at the proline α-amine with several groups that mimic the side chains of natural amino acids, including alanine, leucine, and phenylalanine, is herein described. These γ-peptides enter into different cell lines (COS-1 and HeLa) via an endocytic mechanism. The ability of these compounds to be taken up into cells was studied at 37 °C and 4 °C by plate fluorimetry, flow cytometry, and confocal microscopy. In addition to their capacity for cellular uptake, these unnatural short length oligomers offer advantages over the well-known penetrating TAT peptide, such as being less toxic than TAT and protease resistance.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja051648k