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10.1016/j.jcis.2021.07.072 http://scihub22266oqcxt.onion/10.1016/j.jcis.2021.07.072 34329980!ä!34329980 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Colloid+Interface+Sci 2022 ; 605 (ä): 286-295 Nephropedia Template TP {{tp|p=34329980|t=2022. Modelling the adsorption of proteins to nanoparticles at the solid-liquid interface |pdf=|usr=}}{{34329980}} gab.com Text Modelling the adsorption of proteins to nanoparticles at the solid-liquid interface JO: J Colloid Interface Sci http://www.kidney.de/pget.php?&tw=1&pmid=34329980 #FOAvip HYPOTHESIS: We developed a geometrical model to determine the theoretical maximum number of proteins that can pack as a monolayer surrounding a spherical nanoparticle. We applied our new model to study the adsorption of receptor binding domain (RBD) of the SARS-CoV-2 spike protein to silica nanoparticles. Due to its abundance and extensive use in manufacturing, silica represents a reservoir where the virus can accumulate. It is therefore important to study the adsorption and the persistence of viral components on inanimate surfaces. EXPERIMENTS: We used previously published datasets of nanoparticle-adsorbed proteins to validate the new model. We then used integrated experimental methods and Molecular Dynamics (MD) simulations to characterise binding of the RBD to silica nanoparticles and the effect of such binding on RBD structure. FINDINGS: The new model showed excellent fit with existing datasets and, combined to new RBD-silica nanoparticles binding data, revealed a surface occupancy of 32% with respect to the maximum RBD packing theoretically achievable. Up to 25% of RBD's secondary structures undergo conformational changes as a consequence of adsorption onto silica nanoparticles. Our findings will help developing a better understanding of the principles governing interaction of proteins with surfaces and can contribute to control the spread of SARS-CoV-2 through contaminated objects. Twit Text FOAVip Modelling the adsorption of proteins to nanoparticles at the solid-liquid interface ????J Colloid Interface Sci http://www.kidney.de/pget.php?&tw=1&pmid=34329980 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34329980 #FOAvip English Wikipedia <ref>{{Cite pmid|34329980}}</ref> Modelling the adsorption of proteins to nanoparticles at the solid-liquid interface #MMPMID34329980 Soloviev M; Siligardi G; Roccatano D; Ferrari E J Colloid Interface Sci 2022[Jan]; 605 (ä): 286-295 PMID34329980show ga HYPOTHESIS: We developed a geometrical model to determine the theoretical maximum number of proteins that can pack as a monolayer surrounding a spherical nanoparticle. We applied our new model to study the adsorption of receptor binding domain (RBD) of the SARS-CoV-2 spike protein to silica nanoparticles. Due to its abundance and extensive use in manufacturing, silica represents a reservoir where the virus can accumulate. It is therefore important to study the adsorption and the persistence of viral components on inanimate surfaces. EXPERIMENTS: We used previously published datasets of nanoparticle-adsorbed proteins to validate the new model. We then used integrated experimental methods and Molecular Dynamics (MD) simulations to characterise binding of the RBD to silica nanoparticles and the effect of such binding on RBD structure. FINDINGS: The new model showed excellent fit with existing datasets and, combined to new RBD-silica nanoparticles binding data, revealed a surface occupancy of 32% with respect to the maximum RBD packing theoretically achievable. Up to 25% of RBD's secondary structures undergo conformational changes as a consequence of adsorption onto silica nanoparticles. Our findings will help developing a better understanding of the principles governing interaction of proteins with surfaces and can contribute to control the spread of SARS-CoV-2 through contaminated objects. |*COVID-19[MESH] |*Nanoparticles[MESH] |Adsorption[MESH] |Humans[MESH] |Protein Binding[MESH] |SARS-CoV-2[MESH]Modelling the adsorption of proteins to nanoparticles at the solid-liq(epmc).pdf DeepDyve Pubget Overpricing