Identification and characterization of a novel cell-penetrating peptide of 30Kc19 protein derived from Bombyx mori

Park, Hee Ho; Sohn, Youngsoo; Yeo, Ji Woo; Park, Jae Young; Lee, Hong Jai; Ryu, Jina; Rhee, Won Jong

doi:10.1016/j.procbio.2014.05.008

Cited by 17 publications

(18 citation statements)

References 85 publications

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“…It means that 30Kc19α is 1.4 times higher than 30Kc19 in the cell‐penetrating ability. In our previous work, Pep‐c19 which is a CPP of 30Kc19 was 1.6 times higher than 30Kc19 in the cell‐penetrating ability . This indicates that the penetrating property of 30Kc19α is similar or a little lower than that of Pep‐c19.…”

Section: Resultsmentioning

confidence: 82%

“…Previously, our group reported that 30Kc19 has a cell‐penetrating property regardless of cell type and encompasses a CPP, which was identified as a short peptide with 13 amino acids (Val45‐Cys57) . Thus, we predicted that 30Kc19α may be capable of cell penetration as this CPP is located within the 30Kc19α domain.…”

Section: Resultsmentioning

confidence: 89%

“…HeLa cells were cultured in 96‐well plates (Nunc Lab‐Tek, Thermo Fisher Scientific, Rockford, IL, USA) and incubated with 20 μM of GFP‐30Kc19 or GFP‐30Kc19α protein. GFP‐30Kc19 and GFP‐30Kc19α were expressed and purified from E. coli . Cells were washed three times with PBS and intracellular GFP delivery by 30Kc19 or 30Kc19α was analyzed by measuring GFP fluorescence intensity with a spectrofluorometer.…”

Section: Methodsmentioning

confidence: 99%

“…For instance, incubation of mitochondrial enzyme complex and sialytransferase with 30Kc19 protein increased these enzymes stability and activity . It is interesting that Pep‐c19 which is a cell‐penetrating peptide (CPP) of 30Kc19 does not have homology to other previously reported CPPs , and the dimerization of this Pep‐c19 is the prerequisite for intracellular penetration . Cell‐penetrating proteins can be applied to the in vitro and in vivo delivery of various cargo molecules .…”

Section: Introductionmentioning

confidence: 99%

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Protein‐stabilizing and cell‐penetrating properties of α‐helix domain of 30Kc19 protein

Ryu

Kim

Park

et al. 2016

Biotechnology Journal

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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.

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Section: Resultsmentioning

confidence: 82%

Section: Resultsmentioning

confidence: 89%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Protein‐stabilizing and cell‐penetrating properties of α‐helix domain of 30Kc19 protein

Ryu

Kim

Park

et al. 2016

Biotechnology Journal

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“…A recent study showed that the 30Kc19 protein has cellpenetrating and protein-delivering properties when added to culture medium, due to the presence of cell-penetrating peptide (CPP) in the sequence [48,50]. 30Kc19 and 30Kc6 are part of the so-called "30 K protein" and are similar in terms of size but differentiate with one another in terms of the sequence, structure, and functions.…”

Section: Cell Penetration Of the 30kc19-30kc6 Protein In Cho Cellsmentioning

confidence: 99%

Enhancement of human erythropoietin production in Chinese hamster ovary cells through supplementation of 30Kc19-30Kc6 fusion protein

Park

Choi

Lee

et al. 2015

Process Biochemistry

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Enhancement of Wound Healing Efficacy by Increasing the Stability and Skin‐Penetrating Property of bFGF Using 30Kc19α‐Based Fusion Protein

Lee

Kim

et al. 2021

Advanced Biology

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involvement in tissue growth and regeneration, including wound healing. Activation of FGF receptor by bFGF stimulates intracellular signaling pathways such as phosphoinositide 3-kinase (PI3K)/protein kinase B (Akt) and mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (ERK) signaling pathways which are related to the mitogenic response of cells. [1] As bFGF acts on various target cells involved in wound healing, its effects on wound healing have been extensively studied. [2] bFGF promotes the migration of dermal fibroblasts, keratinocytes, and endothelial cells, into wound sites and facilitates their proliferation. [3] As a result, bFGF accelerates granulation tissue formation and angiogenesis, which results in matrix formation and remodeling. [4] In recent years, a number of clinical uses of recombinant bFGF have been reported, and these include treatment of chronic wounds, second-degree burns, pressure ulcers, and diabetic foot ulcers. [5] However, its inherent instability and rapid degradation often require frequent treatments in tandem with higher concentrations. [6] The reported half-life of recombinant bFGF is less than 10 h under normal cell culture conditions and even shorter in the living organisms, which significantly limits The instability of recombinant basic fibroblast growth factor (bFGF) is a major disadvantage for its therapeutic use and means frequent applications to cells or tissues are required for sustained effects. Originating from silkworm hemolymph, 30Kc19α is a cell-penetrating protein that also has protein stabilization properties. Herein, it is investigated whether fusing 30Kc19α to bFGF can enhance the stability and skin penetration properties of bFGF, which may consequently increase its therapeutic efficacy. The fusion of 30Kc19α to bFGF protein increases protein stability, as confirmed by ELISA. 30Kc19α-bFGF also retains the biological activity of bFGF as it facilitates the migration and proliferation of fibroblasts and angiogenesis of endothelial cells. It is discovered that 30Kc19α can improve the transdermal delivery of a small molecular fluorophore through the skin of hairless mice. Importantly, it increases the accumulation of bFGF and further facilitates its translocation into the skin through follicular routes. Finally, when applied to a skin wound model in vivo, 30Kc19α-bFGF penetrates the dermis layer effectively, which promotes cell proliferation, tissue granulation, angiogenesis, and tissue remodeling. Consequently, the findings suggest that 30Kc19α improves the therapeutic functionalities of bFGF, and would be useful as a protein stabilizer and/or a delivery vehicle in therapeutic applications.

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Identification and characterization of a novel cell-penetrating peptide of 30Kc19 protein derived from Bombyx mori

Cited by 17 publications

References 85 publications

Protein‐stabilizing and cell‐penetrating properties of α‐helix domain of 30Kc19 protein

Protein‐stabilizing and cell‐penetrating properties of α‐helix domain of 30Kc19 protein

Enhancement of human erythropoietin production in Chinese hamster ovary cells through supplementation of 30Kc19-30Kc6 fusion protein

Enhancement of Wound Healing Efficacy by Increasing the Stability and Skin‐Penetrating Property of bFGF Using 30Kc19α‐Based Fusion Protein

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