We reported a new vector-carrier-cargo platform called lipoproplex, schematically represented in the Figure , and demonstrated its ability to transport active proteins through the cell membrane. For this purpose, we used DNA nanogels cross-linked via streptavidin-biotin interactions. This platform enables loading of the protein cargo into DNA carrier in several ways (i.e. using streptavidinated, biotinylated or strep-tagged cargo proteins) thus opening the possibility of large number of functionalities that can be potentially introduced into a single nanogel. We used cationic liposomes for the vectorization of DNA-protein NGs and renamed the resulting complex as "lipoproplex", which evokes the complex between DNA and liposomes (i.e. lipoplex) but is intended to emphasize the importance of the protein component in our DNA-protein nanogels. Three-dimensional structure of the nanogels demands lower concentration of cationic liposomes for complexation (down to R+/-= 0.75), which in combination with intrinsic biocompatibility of DNA nanoscaffold results in non-toxic protein delivery system as demonstrated by the MTT assay. For a proof of concept, here we investigated delivery of two proteins: biotinylated fluorescent protein GFP and the enzyme alkaline phosphatase conjugated to streptavidin. In both cases, the complexation with cationic liposomes and subsequent internalization by the cells did not affect the respective properties of the proteins: GFP retained its fluorescence emission whereas the ALP kept its efficiency to hydrolyze the DDAO-P substrate. Both strategies thus proved to be adapted for the nanogels functionalization.