Λεπτομέρειες βιβλιογραφικής εγγραφής
| Τίτλος: |
Dendrimer end-terminal motif-dependent evasion of human complement and complement activation through IgM hitchhiking |
| Συγγραφείς: |
Wu L-P, Ficker M, Christensen JB, Simberg D, Trohopoulos PN, Moghimi SM |
| Πηγή: |
Nature Communications, December 2021 |
| Στοιχεία εκδότη: |
Nature Research |
| Έτος έκδοσης: |
2021 |
| Συλλογή: |
Newcastle University Library ePrints Service |
| Περιγραφή: |
© 2021, The Author(s).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. |
| Τύπος εγγράφου: |
article in journal/newspaper |
| Περιγραφή αρχείου: |
application/pdf |
| Γλώσσα: |
unknown |
| Relation: |
https://eprints.ncl.ac.uk/276634; https://eprints.ncl.ac.uk/fulltext.aspx?url=276634/EFB3FA0A-205D-4FBF-8319-A9B2DA594558.pdf&pub_id=276634 |
| Διαθεσιμότητα: |
https://eprints.ncl.ac.uk/276634 |
| Rights: |
https://creativecommons.org/licenses/by/4.0/ |
| Αριθμός Καταχώρησης: |
edsbas.E6FC86C1 |
| Βάση Δεδομένων: |
BASE |