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A C-terminal peptide of TFPI-1 facilitates cytosolic delivery of nucleic acid cargo into mammalian cells

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Fazil, Mobashar Hussain Urf Turabe ; Chalasani, Madhavi Latha Somaraju ; Choong, Yeu Khai ; Schmidtchen, Artur ; Verma, Navin Kumar ; Saravanan, Rathi. / A C-terminal peptide of TFPI-1 facilitates cytosolic delivery of nucleic acid cargo into mammalian cells. I: Biochimica et Biophysica Acta - Biomembranes. 2020 ; Bind 1862, Nr. 2. s. 183093.

Bibtex

@article{93de1a7b2d474a21a348439fb9be4432,
title = "A C-terminal peptide of TFPI-1 facilitates cytosolic delivery of nucleic acid cargo into mammalian cells",
abstract = "Efficient intracellular nucleic acid delivery into mammalian cells remains a long-standing challenge owing to poor cell permeability and uptake of naked nucleic acids across the cell membrane and limited cargo stability. Conventional delivery methods have several drawbacks, such as cytotoxicity, limited cell-type applicability, low efficiency, hindrances that limit the potential of oligonucleotide delivery in functional genomics, therapeutics and diverse research applications. Thus, new approaches that are robust, safe, effective and valid across multiple cell types are much needed. Here, we demonstrate that GGL27, a TFPI-1-derived novel cationic host defence peptide, facilitates the delivery of nucleic acid cargo into the cytosol of a range of mammalian cells. The GGL27 peptide is non-cytotoxic and is internalized in a broad range of mammalian cell-types, including transformed cell lines and primary cells. GGL27 spontaneously forms complexes with nucleic acids of variable sizes, protects them from nuclease degradation, and delivers cargo effectively. Together, our observations demonstrate the versatile cell-penetrating property of GGL27, providing an excellent template for developing a simple, non-toxic peptide-based cytosolic delivery tool for wide use in biomedical research.",
keywords = "Animals, Cations, Cell-Penetrating Peptides/pharmacology, Cytosol/metabolism, Drug Delivery Systems/methods, Humans, Lipoproteins/metabolism, Mammals, Nucleic Acids/metabolism, Peptides, Intracellular gene delivery, Host defence peptide, Nucleic acid therapeutics",
author = "Fazil, {Mobashar Hussain Urf Turabe} and Chalasani, {Madhavi Latha Somaraju} and Choong, {Yeu Khai} and Artur Schmidtchen and Verma, {Navin Kumar} and Rathi Saravanan",
note = "Copyright {\textcopyright} 2019 Elsevier B.V. All rights reserved.",
year = "2020",
month = feb,
day = "1",
doi = "10.1016/j.bbamem.2019.183093",
language = "English",
volume = "1862",
pages = "183093",
journal = "Biochimica et Biophysica Acta - Biomembranes",
issn = "0005-2736",
publisher = "Elsevier BV",
number = "2",

}

RIS

TY - JOUR

T1 - A C-terminal peptide of TFPI-1 facilitates cytosolic delivery of nucleic acid cargo into mammalian cells

AU - Fazil, Mobashar Hussain Urf Turabe

AU - Chalasani, Madhavi Latha Somaraju

AU - Choong, Yeu Khai

AU - Schmidtchen, Artur

AU - Verma, Navin Kumar

AU - Saravanan, Rathi

N1 - Copyright © 2019 Elsevier B.V. All rights reserved.

PY - 2020/2/1

Y1 - 2020/2/1

N2 - Efficient intracellular nucleic acid delivery into mammalian cells remains a long-standing challenge owing to poor cell permeability and uptake of naked nucleic acids across the cell membrane and limited cargo stability. Conventional delivery methods have several drawbacks, such as cytotoxicity, limited cell-type applicability, low efficiency, hindrances that limit the potential of oligonucleotide delivery in functional genomics, therapeutics and diverse research applications. Thus, new approaches that are robust, safe, effective and valid across multiple cell types are much needed. Here, we demonstrate that GGL27, a TFPI-1-derived novel cationic host defence peptide, facilitates the delivery of nucleic acid cargo into the cytosol of a range of mammalian cells. The GGL27 peptide is non-cytotoxic and is internalized in a broad range of mammalian cell-types, including transformed cell lines and primary cells. GGL27 spontaneously forms complexes with nucleic acids of variable sizes, protects them from nuclease degradation, and delivers cargo effectively. Together, our observations demonstrate the versatile cell-penetrating property of GGL27, providing an excellent template for developing a simple, non-toxic peptide-based cytosolic delivery tool for wide use in biomedical research.

AB - Efficient intracellular nucleic acid delivery into mammalian cells remains a long-standing challenge owing to poor cell permeability and uptake of naked nucleic acids across the cell membrane and limited cargo stability. Conventional delivery methods have several drawbacks, such as cytotoxicity, limited cell-type applicability, low efficiency, hindrances that limit the potential of oligonucleotide delivery in functional genomics, therapeutics and diverse research applications. Thus, new approaches that are robust, safe, effective and valid across multiple cell types are much needed. Here, we demonstrate that GGL27, a TFPI-1-derived novel cationic host defence peptide, facilitates the delivery of nucleic acid cargo into the cytosol of a range of mammalian cells. The GGL27 peptide is non-cytotoxic and is internalized in a broad range of mammalian cell-types, including transformed cell lines and primary cells. GGL27 spontaneously forms complexes with nucleic acids of variable sizes, protects them from nuclease degradation, and delivers cargo effectively. Together, our observations demonstrate the versatile cell-penetrating property of GGL27, providing an excellent template for developing a simple, non-toxic peptide-based cytosolic delivery tool for wide use in biomedical research.

KW - Animals

KW - Cations

KW - Cell-Penetrating Peptides/pharmacology

KW - Cytosol/metabolism

KW - Drug Delivery Systems/methods

KW - Humans

KW - Lipoproteins/metabolism

KW - Mammals

KW - Nucleic Acids/metabolism

KW - Peptides

KW - Intracellular gene delivery

KW - Host defence peptide

KW - Nucleic acid therapeutics

UR - http://www.scopus.com/inward/record.url?scp=85075425649&partnerID=8YFLogxK

U2 - 10.1016/j.bbamem.2019.183093

DO - 10.1016/j.bbamem.2019.183093

M3 - Journal article

C2 - 31672541

VL - 1862

SP - 183093

JO - Biochimica et Biophysica Acta - Biomembranes

JF - Biochimica et Biophysica Acta - Biomembranes

SN - 0005-2736

IS - 2

M1 - 183093

ER -

ID: 61845869