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Protein‐stabilizing and cell‐penetrating properties of α‐helix domain of 30Kc19 protein
Author(s) -
Ryu Jina,
Kim Hyoju,
Park Hee Ho,
Lee Hong Jai,
Park Ju Hyun,
Rhee Won Jong,
Park Tai Hyun
Publication year - 2016
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.201600040
Subject(s) - helix (gastropod) , cell , protein domain , biophysics , chemistry , domain (mathematical analysis) , protein structure , cytotoxicity , protein engineering , microbiology and biotechnology , biochemistry , biology , in vitro , enzyme , ecology , mathematical analysis , mathematics , snail , gene
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.