The protein-stabilizing and cell-penetrating activities of Bombyx mori 30Kc19 α-helix domain (30Kc19α) are investigated. Recently, 30Kc19 protein has been studied extensively as it has both protein-stabilizing and cell-penetrating properties. However, it is unknown which part of 30Kc19 is responsible for those properties. 30Kc19 protein is composed of two distinct domains, an α-helix N-terminal domain (30Kc19α) and a β-trefoil C-terminal domain (30Kc19β). The authors construct and produce truncated forms of 30Kc19 to demonstrate their biological functions. Interestingly, 30Kc19α was shown to be responsible for both the protein-stabilizing and cell-penetrating properties of 30Kc19 protein. 30Kc19α shows even higher protein delivery activity than did whole 30Kc19 protein and has low cytotoxicity when added to cell culture medium. Therefore, based on its multifunctional properties, 30Kc19α can be developed as a novel candidate for a therapeutic protein carrier into various cells and tissues.
Bibliographical noteFunding Information:
This study was supported by the National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT, and Future Planning (2015061592). The authors declare no financial or commercial conflict of interest.
© 2016 The Authors. Biotechnology Journal published by WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
- Drug delivery
- Protein stability