China Agricultural University, China
Title: Engineering protein interfaces yields ferritin disassembly and reassembly under benign experimental conditions
Biography: Hai Chen
Ferritin is a class of naturally occurring iron storage protein; it usually consists of 24 subunits that form a hollow protein shell with high symmetry. Recently, scientists have subverted these nature functions and used reversibly self-assembled property of apoferritin cage controlled by pH for the encapsulation and delivery of bioactive nutrients or anticancer drug. In all these cases, the ferritin cages shield their cargo from the influence of external conditions and provide a controlled microenvironment. However, since ferritin disassociation generally needs extreme acidic condition (pH≤2), this strategy is limited to the structures of bioactive compounds that are unstable at such low pH. Here, we engineered protein interfaces to yield ferritin nano cages which disassemble at pH 4.0 and reassemble at pH 7.5. During this process, bioactive molecules can be encapsulated within protein cavity. Thus, this engineered protein has the potential to be exploited as an alternative nano carrier for pH-sensitive bioactive compounds or drugs.