Protein‐stabilizing and cell‐penetrating properties of α‐helix domain of 30Kc19 protein. Issue 11 (12th August 2016) - Ryu, Jina
Abstract: 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. Abstract : 30Kc19 protein is composed of two distinct domains, an α‐helix N‐terminal domain (30Kc19α) and a β‐trefoil C‐terminal domain (30Kc19β). Here it's demonstrated that 30Kc19α has multifunctional properties, which are cell penetration, stabilization, and cargo delivery. The potential of 30Kc19α as a novel candidate for a therapeutic protein carrier into various cells and tissues is shown. This article is part of an AFOB (Asian Federation of Biotechnology) Special issue. To learn more about the AFOB, visitwww.afob.org .