Protein folding is very complicated mechanism, so it is still mysterious even though DNA transcription or translation step is quite well known. Thus, many scientists have tried to understand protein folding, and one of the major achievement is discovery of molecular chaperones. However, molecular chaperones have an effect on only small portion of total protein. To explain folding of majority protein, we hypothesized anti-aggregation activity of macromolecular interactions via steric hindrance effect and charge effect. In this presentation, I used artificial macromolecular interaction rather than natural interaction partners, so I excluded induced fit conformational change effect and focused on steric hindrance effect and charge effect on protein folding. Then I confirmed that induced artificial macromolecular interaction can help folding of diverse kinds of protein.