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Protein and peptide delivery via engineered polyomavirus‐like particles
Author(s) -
Günther Constanze,
Schmidt Uli,
Rudolph Rainer,
Böhm Gerald
Publication year - 2001
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.00-0645fje
Subject(s) - peptide , chemistry , virology , biology , biochemistry
Recent advances in molecular biology have led to the development of new therapeutics to address genetic disorders. The developments in the production and availability of recombinant proteins are likely to have a substantial impact on many diseases in the short term. A major limit for the use of recombinant proteins in clinical applications is their inability to enter cells and be targeted to the appropriate intracellular site. Here, we describe a novel system for the intracellular delivery of peptides and proteins using recombinantly expressed polyomavirus‐like particles as universal carriers. The inner surface of the particles was modified by the fusion of a WW domain, which was derived from the mouse formin binding protein 11 (FBP11) to the viral coat protein in order to bind specifically to proline‐rich ligands. Physicochemical characterization of the fusion protein demonstrated that the functional units of the VP1‐WW protein remained intact. Assembly of the particles in the presence of proline‐rich ligands resulted in an efficient encapsidation of the ligands into the particles. Fluorescence‐labeled peptides and the green fluorescent protein were used as model ligands. The delivery of the ligands into cultured eukaryotic cells could be demonstrated with confocal laser‐scanning microscopy.