Dendrimer end-terminal motif-dependent evasion of human complement and complement activation through IgM hitchhiking

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Standard

Dendrimer end-terminal motif-dependent evasion of human complement and complement activation through IgM hitchhiking. / Wu, Lin Ping; Ficker, Mario; Christensen, Jørn B.; Simberg, Dmitri; Trohopoulos, Panagiotis N.; Moghimi, Seyed M.

I: Nature Communications, Bind 12, Nr. 1, 4858, 12.2021.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Wu, LP, Ficker, M, Christensen, JB, Simberg, D, Trohopoulos, PN & Moghimi, SM 2021, 'Dendrimer end-terminal motif-dependent evasion of human complement and complement activation through IgM hitchhiking', Nature Communications, bind 12, nr. 1, 4858. https://doi.org/10.1038/s41467-021-24960-6

APA

Wu, L. P., Ficker, M., Christensen, J. B., Simberg, D., Trohopoulos, P. N., & Moghimi, S. M. (2021). Dendrimer end-terminal motif-dependent evasion of human complement and complement activation through IgM hitchhiking. Nature Communications, 12(1), [4858]. https://doi.org/10.1038/s41467-021-24960-6

Vancouver

Wu LP, Ficker M, Christensen JB, Simberg D, Trohopoulos PN, Moghimi SM. Dendrimer end-terminal motif-dependent evasion of human complement and complement activation through IgM hitchhiking. Nature Communications. 2021 dec.;12(1). 4858. https://doi.org/10.1038/s41467-021-24960-6

Author

Wu, Lin Ping ; Ficker, Mario ; Christensen, Jørn B. ; Simberg, Dmitri ; Trohopoulos, Panagiotis N. ; Moghimi, Seyed M. / Dendrimer end-terminal motif-dependent evasion of human complement and complement activation through IgM hitchhiking. I: Nature Communications. 2021 ; Bind 12, Nr. 1.

Bibtex

@article{3012100a4ba74d9481c26b5e254a5991,
title = "Dendrimer end-terminal motif-dependent evasion of human complement and complement activation through IgM hitchhiking",
abstract = "Complement is an enzymatic humoral pattern-recognition defence system of the body. Non-specific deposition of blood biomolecules on nanomedicines triggers complement activation through the alternative pathway, but complement-triggering mechanisms of nanomaterials with dimensions comparable to or smaller than many globular blood proteins are unknown. Here we study this using a library of <6 nm poly(amido amine) dendrimers bearing different end-terminal functional groups. Dendrimers are not sensed by C1q and mannan-binding lectin, and hence do not trigger complement activation through these pattern-recognition molecules. While, pyrrolidone- and carboxylic acid-terminated dendrimers fully evade complement response, and independent of factor H modulation, binding of amine-terminated dendrimers to a subset of natural IgM glycoforms triggers complement activation through lectin pathway-IgM axis. These findings contribute to mechanistic understanding of complement surveillance of dendrimeric materials, and provide opportunities for dendrimer-driven engineering of complement-safe nanomedicines and medical devices.",
author = "Wu, {Lin Ping} and Mario Ficker and Christensen, {J{\o}rn B.} and Dmitri Simberg and Trohopoulos, {Panagiotis N.} and Moghimi, {Seyed M.}",
note = "Publisher Copyright: {\textcopyright} 2021, The Author(s).",
year = "2021",
month = dec,
doi = "10.1038/s41467-021-24960-6",
language = "English",
volume = "12",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - Dendrimer end-terminal motif-dependent evasion of human complement and complement activation through IgM hitchhiking

AU - Wu, Lin Ping

AU - Ficker, Mario

AU - Christensen, Jørn B.

AU - Simberg, Dmitri

AU - Trohopoulos, Panagiotis N.

AU - Moghimi, Seyed M.

N1 - Publisher Copyright: © 2021, The Author(s).

PY - 2021/12

Y1 - 2021/12

N2 - Complement is an enzymatic humoral pattern-recognition defence system of the body. Non-specific deposition of blood biomolecules on nanomedicines triggers complement activation through the alternative pathway, but complement-triggering mechanisms of nanomaterials with dimensions comparable to or smaller than many globular blood proteins are unknown. Here we study this using a library of <6 nm poly(amido amine) dendrimers bearing different end-terminal functional groups. Dendrimers are not sensed by C1q and mannan-binding lectin, and hence do not trigger complement activation through these pattern-recognition molecules. While, pyrrolidone- and carboxylic acid-terminated dendrimers fully evade complement response, and independent of factor H modulation, binding of amine-terminated dendrimers to a subset of natural IgM glycoforms triggers complement activation through lectin pathway-IgM axis. These findings contribute to mechanistic understanding of complement surveillance of dendrimeric materials, and provide opportunities for dendrimer-driven engineering of complement-safe nanomedicines and medical devices.

AB - Complement is an enzymatic humoral pattern-recognition defence system of the body. Non-specific deposition of blood biomolecules on nanomedicines triggers complement activation through the alternative pathway, but complement-triggering mechanisms of nanomaterials with dimensions comparable to or smaller than many globular blood proteins are unknown. Here we study this using a library of <6 nm poly(amido amine) dendrimers bearing different end-terminal functional groups. Dendrimers are not sensed by C1q and mannan-binding lectin, and hence do not trigger complement activation through these pattern-recognition molecules. While, pyrrolidone- and carboxylic acid-terminated dendrimers fully evade complement response, and independent of factor H modulation, binding of amine-terminated dendrimers to a subset of natural IgM glycoforms triggers complement activation through lectin pathway-IgM axis. These findings contribute to mechanistic understanding of complement surveillance of dendrimeric materials, and provide opportunities for dendrimer-driven engineering of complement-safe nanomedicines and medical devices.

U2 - 10.1038/s41467-021-24960-6

DO - 10.1038/s41467-021-24960-6

M3 - Journal article

C2 - 34381048

AN - SCOPUS:85112345371

VL - 12

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 4858

ER -

ID: 279126591