scholarly journals Exploring Cellular Interactions of Liposomes Using Protein Corona Fingerprints and Physicochemical Properties

ACS Nano ◽  
2016 ◽  
Vol 10 (3) ◽  
pp. 3723-3737 ◽  
Author(s):  
Arafeh Bigdeli ◽  
Sara Palchetti ◽  
Daniela Pozzi ◽  
Mohammad Reza Hormozi-Nezhad ◽  
Francesca Baldelli Bombelli ◽  
...  
2018 ◽  
Vol 5 (1) ◽  
pp. 64-71 ◽  
Author(s):  
Matthew R. Findlay ◽  
Daniel N. Freitas ◽  
Maryam Mobed-Miremadi ◽  
Korin E. Wheeler

Proteins encountered in biological and environmental systems bind to engineered nanomaterials (ENMs) to form a protein corona (PC) that alters the surface chemistry, reactivity, and fate of the ENMs.


2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Michael P. Vincent ◽  
Sharan Bobbala ◽  
Nicholas B. Karabin ◽  
Molly Frey ◽  
Yugang Liu ◽  
...  

AbstractControlling 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.


2020 ◽  
Author(s):  
Michael P. Vincent ◽  
Sharan Bobbala ◽  
Nicholas B. Karabin ◽  
Molly Frey ◽  
Yugang Liu ◽  
...  

AbstractControlling 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 the dominant protein to adsorb to nanobiomaterial surfaces, a process that is considered benign or beneficial by minimizing opsonization or inflammation. Here, we demonstrate the surface chemistry of a model self-assembled 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 were found to promote albumin recognition by macrophage class A1 scavenger receptors (SR-A1), 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.


Nanomaterials ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 3214
Author(s):  
Edward Sacher ◽  
Arthur Yelon

A consideration of the antibacterial efficacy of metal-based nanoparticles, from the point of view of their physicochemical properties, suggests that such efficacy arises from the protein coronas that form around them, and that the contents of the coronas depend on the chemical groups found on the nanoparticle surfaces. We offer a new perspective and new insights, making use of our earlier observations of the physicochemical properties of nanoparticle surfaces, to propose that the nanoparticle serves as a mediator for the formation and activation of the protein corona, which attacks the bacterium. That is, the nanoparticle enhances the body’s natural defenses, using proteins present in body fluids.


Toxicology ◽  
2020 ◽  
Vol 442 ◽  
pp. 152545
Author(s):  
Alejandro Déciga-Alcaraz ◽  
Estefany I. Medina-Reyes ◽  
Norma L. Delgado-Buenrostro ◽  
Carolina Rodríguez-Ibarra ◽  
Adriana Ganem-Rondero ◽  
...  

Author(s):  
Xing Li ◽  
Erkai He ◽  
Bing Xia ◽  
Yang Liu ◽  
Peihua Zhang ◽  
...  

Nanoplastics contamination is one of the pressing environmental concerns globally. Among many environmental factors in the aquatic system, ubiquitous proteins are expected to affect the physicochemical properties of nanoplastics, and...


2014 ◽  
Vol 5 ◽  
pp. 1699-1711 ◽  
Author(s):  
Wolfgang G Kreyling ◽  
Stefanie Fertsch-Gapp ◽  
Martin Schäffler ◽  
Blair D Johnston ◽  
Nadine Haberl ◽  
...  

When particles incorporated within a mammalian organism come into contact with body fluids they will bind to soluble proteins or those within cellular membranes forming what is called a protein corona. This binding process is very complex and highly dynamic due to the plethora of proteins with different affinities and fractions in different body fluids and the large variation of compounds and structures of the particle surface. Interestingly, in the case of nanoparticles (NP) this protein corona is well suited to provide a guiding vehicle of translocation within body fluids and across membranes. This NP translocation may subsequently lead to accumulation in various organs and tissues and their respective cell types that are not expected to accumulate such tiny foreign bodies. Because of this unprecedented NP accumulation, potentially adverse biological responses in tissues and cells cannot be neglected a priori but require thorough investigations. Therefore, we studied the interactions and protein binding kinetics of blood serum proteins with a number of engineered NP as a function of their physicochemical properties. Here we show by in vitro incubation tests that the binding capacity of different engineered NP (polystyrene, elemental carbon) for selected serum proteins depends strongly on the NP size and the properties of engineered surface modifications. In the following attempt, we studied systematically the effect of the size (5, 15, 80 nm) of gold spheres (AuNP), surface-modified with the same ionic ligand; as well as 5 nm AuNP with five different surface modifications on the binding to serum proteins by using proteomics analyses. We found that the binding of numerous serum proteins depended strongly on the physicochemical properties of the AuNP. These in vitro results helped us substantially in the interpretation of our numerous in vivo biokinetics studies performed in rodents using the same NP. These had shown that not only the physicochemical properties determined the AuNP translocation from the organ of intake towards blood circulation and subsequent accumulation in secondary organs and tissues but also the the transport across organ membranes depended on the route of AuNP application. Our in vitro protein binding studies support the notion that the observed differences in in vivo biokinetics are mediated by the NP protein corona and its dynamical change during AuNP translocation in fluids and across membranes within the organism.


Small ◽  
2016 ◽  
Vol 12 (13) ◽  
pp. 1758-1769 ◽  
Author(s):  
Andrzej S. Pitek ◽  
Amy M. Wen ◽  
Sourabh Shukla ◽  
Nicole F. Steinmetz

Author(s):  
Víctor F. Puntes ◽  
Joan Comenge

<p>Although nanoparticles have been traditionally modified with a single ligand layer, mixture of ligands might help to combine different functionalities and to further engineer the NP surface. A detailed study of the competition between an alkanethiol (11-mercaptoundecanoic acid) and SH-PEG for the surface of AuNPs and the resultant behaviors of this model nanoconjugate is presented here. As a result, the physicochemical properties of these conjugates can be progressively tuned by controlling the composition and especially the conformation of the mixed monolayer. This has implications in the physiological stability. The controlled changes on the SH-PEG conformation rather than its concentration induces a change in the stabilization mechanism from electrostatic repulsion to steric hindrance, which changes the biological fate of NPs. Importantly, the adsorption of proteins on the conjugates can be tailored by tuning the composition and conformation of the mixed layer.</p>


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