Surface chemistry-mediated modulation of adsorbed albumin folding state specifies nanocarrier clearance by distinct macrophage subsets

Michael P. Vincent, Sharan Bobbala, Nicholas B. Karabin, Molly Frey, Yugang Liu, Justin O. Navidzadeh, Trevor Stack and Evan A. Scott ()
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Michael P. Vincent: Northwestern University
Sharan Bobbala: Northwestern University
Nicholas B. Karabin: Northwestern University
Molly Frey: Northwestern University
Yugang Liu: Northwestern University
Justin O. Navidzadeh: Northwestern University
Trevor Stack: Northwestern University
Evan A. Scott: Northwestern University

Nature Communications, 2021, vol. 12, issue 1, 1-18

Abstract: Abstract Controlling nanocarrier interactions with the immune system requires a thorough understanding of the surface properties that modulate protein adsorption in biological fluids, since the resulting protein corona redefines cellular interactions with nanocarrier surfaces. Albumin is initially one of the dominant proteins to adsorb to nanocarrier surfaces, a process that is considered benign or beneficial by minimizing opsonization or inflammation. Here, we demonstrate the surface chemistry of a model nanocarrier can be engineered to stabilize or denature the three-dimensional conformation of adsorbed albumin, which respectively promotes evasion or non-specific clearance in vivo. Interestingly, certain common chemistries that have long been considered to convey stealth properties denature albumin to promote nanocarrier recognition by macrophage class A1 scavenger receptors, providing a means for their eventual removal from systemic circulation. We establish that the surface chemistry of nanocarriers can be specified to modulate adsorbed albumin structure and thereby tune clearance by macrophage scavenger receptors.

Date: 2021
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DOI: 10.1038/s41467-020-20886-7

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