Open AccessChaperonin–Dendrimer Conjugates for siRNA Delivery
Author(s) -
Nussbaumer Martin G.,
Duskey Jason T.,
Rother Martin,
Renggli Kasper,
Chami Mohamed,
Bruns Nico
Publication year - 2016
Publication title -
advanced science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.388
H-Index - 100
ISSN - 2198-3844
DOI - 10.1002/advs.201600046
Subject(s) - transfection , small interfering rna , chaperonin , rnase p , chemistry , dendrimer , rna , rna interference , conjugate , microbiology and biotechnology , biophysics , biochemistry , protein folding , biology , mathematical analysis , mathematics , gene
The group II chaperonin thermosome (THS) is a hollow protein nanoparticle that can encapsulate macromolecular guests. Two large pores grant access to the interior of the protein cage. Poly(amidoamine) (PAMAM) is conjugated into THS to act as an anchor for small interfering RNA (siRNA), allowing to load the THS with therapeutic payload. THS–PAMAM protects siRNA from degradation by RNase A and traffics KIF11 and GAPDH siRNA into U87 cancer cells. By modification of the protein cage with the cell‐penetrating peptide TAT, RNA interference is also induced in PC‐3 cells. THS–PAMAM protein–polymer conjugates are therefore promising siRNA transfection reagents and greatly expand the scope of protein cages in drug delivery applications.