Understanding the Adsorption of Peptides and Proteins onto PEGylated Gold Nanoparticles
Polyethylene glycol (PEG) surface conjugations are widely employed to render passivating properties to nanoparticles in biological applications. The benefits of surface passivation by PEG are reduced protein adsorption, diminished non-specific interactions, and improvement in pharmacokinetics. Howev...
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MDPI AG
2021-09-01
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Series: | Molecules |
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Online Access: | https://www.mdpi.com/1420-3049/26/19/5788 |
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author | Yasiru Randika Perera Joanna Xiuzhu Xu Dhanush L. Amarasekara Alex C. Hughes Ibraheem Abbood Nicholas C. Fitzkee |
author_facet | Yasiru Randika Perera Joanna Xiuzhu Xu Dhanush L. Amarasekara Alex C. Hughes Ibraheem Abbood Nicholas C. Fitzkee |
author_sort | Yasiru Randika Perera |
collection | DOAJ |
description | Polyethylene glycol (PEG) surface conjugations are widely employed to render passivating properties to nanoparticles in biological applications. The benefits of surface passivation by PEG are reduced protein adsorption, diminished non-specific interactions, and improvement in pharmacokinetics. However, the limitations of PEG passivation remain an active area of research, and recent examples from the literature demonstrate how PEG passivation can fail. Here, we study the adsorption amount of biomolecules to PEGylated gold nanoparticles (AuNPs), focusing on how different protein properties influence binding. The AuNPs are PEGylated with three different sizes of conjugated PEG chains, and we examine interactions with proteins of different sizes, charges, and surface cysteine content. The experiments are carried out in vitro at physiologically relevant timescales to obtain the adsorption amounts and rates of each biomolecule on AuNP-PEGs of varying compositions. Our findings are relevant in understanding how protein size and the surface cysteine content affect binding, and our work reveals that cysteine residues can dramatically increase adsorption rates on PEGylated AuNPs. Moreover, shorter chain PEG molecules passivate the AuNP surface more effectively against all protein types. |
first_indexed | 2024-03-10T06:54:38Z |
format | Article |
id | doaj.art-0a21dde582a84c208abf295cf52d732d |
institution | Directory Open Access Journal |
issn | 1420-3049 |
language | English |
last_indexed | 2024-03-10T06:54:38Z |
publishDate | 2021-09-01 |
publisher | MDPI AG |
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series | Molecules |
spelling | doaj.art-0a21dde582a84c208abf295cf52d732d2023-11-22T16:32:42ZengMDPI AGMolecules1420-30492021-09-012619578810.3390/molecules26195788Understanding the Adsorption of Peptides and Proteins onto PEGylated Gold NanoparticlesYasiru Randika Perera0Joanna Xiuzhu Xu1Dhanush L. Amarasekara2Alex C. Hughes3Ibraheem Abbood4Nicholas C. Fitzkee5Department of Chemistry, Mississippi State University, Starkville, MS 39762, USADepartment of Chemistry, Mississippi State University, Starkville, MS 39762, USADepartment of Chemistry, Mississippi State University, Starkville, MS 39762, USADepartment of Chemistry, Mississippi State University, Starkville, MS 39762, USADepartment of Chemistry, University of Arkansas at Little Rock, Little Rock, AR 72204, USADepartment of Chemistry, Mississippi State University, Starkville, MS 39762, USAPolyethylene glycol (PEG) surface conjugations are widely employed to render passivating properties to nanoparticles in biological applications. The benefits of surface passivation by PEG are reduced protein adsorption, diminished non-specific interactions, and improvement in pharmacokinetics. However, the limitations of PEG passivation remain an active area of research, and recent examples from the literature demonstrate how PEG passivation can fail. Here, we study the adsorption amount of biomolecules to PEGylated gold nanoparticles (AuNPs), focusing on how different protein properties influence binding. The AuNPs are PEGylated with three different sizes of conjugated PEG chains, and we examine interactions with proteins of different sizes, charges, and surface cysteine content. The experiments are carried out in vitro at physiologically relevant timescales to obtain the adsorption amounts and rates of each biomolecule on AuNP-PEGs of varying compositions. Our findings are relevant in understanding how protein size and the surface cysteine content affect binding, and our work reveals that cysteine residues can dramatically increase adsorption rates on PEGylated AuNPs. Moreover, shorter chain PEG molecules passivate the AuNP surface more effectively against all protein types.https://www.mdpi.com/1420-3049/26/19/5788NMR spectroscopygold nanoparticlesPEGylationadsorptionpassivation |
spellingShingle | Yasiru Randika Perera Joanna Xiuzhu Xu Dhanush L. Amarasekara Alex C. Hughes Ibraheem Abbood Nicholas C. Fitzkee Understanding the Adsorption of Peptides and Proteins onto PEGylated Gold Nanoparticles Molecules NMR spectroscopy gold nanoparticles PEGylation adsorption passivation |
title | Understanding the Adsorption of Peptides and Proteins onto PEGylated Gold Nanoparticles |
title_full | Understanding the Adsorption of Peptides and Proteins onto PEGylated Gold Nanoparticles |
title_fullStr | Understanding the Adsorption of Peptides and Proteins onto PEGylated Gold Nanoparticles |
title_full_unstemmed | Understanding the Adsorption of Peptides and Proteins onto PEGylated Gold Nanoparticles |
title_short | Understanding the Adsorption of Peptides and Proteins onto PEGylated Gold Nanoparticles |
title_sort | understanding the adsorption of peptides and proteins onto pegylated gold nanoparticles |
topic | NMR spectroscopy gold nanoparticles PEGylation adsorption passivation |
url | https://www.mdpi.com/1420-3049/26/19/5788 |
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