Spontaneous desorption of protein from self-assembled monolayer (SAM)-coated gold nanoparticles induced by high temperature

Wang, Shuai; Ou, Xinwen; Yi, Ming; Li, Jingyuan

doi:10.1039/d1cp04000f

Cited by 2 publications

(3 citation statements)

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“…After allowing 1 h for protein exchange at the elevated temperature, less protein exchange was recorded compared to the same experiment carried out at room temperature (22 °C) (Figure ). While protein adsorption rate has been shown to increase at elevated temperatures, ,− these results suggest slower desorption rates at elevated temperatures. Protein exchange on a AuNP surface has been described as an associative exchange mechanism, where the competing protein, e.g., IgG, first adsorbs onto the AuNP surface, followed by the subsequent desorption of the HSA or T-HSA molecule. , At elevated temperatures, the pre-adsorbed protein is more likely to undergo slight thermal unfolding or exhibit increased flexibility resulting in an increase in contact area with the AuNP .…”

Section: Results and Discussionmentioning

confidence: 98%

Controlled Temporal Release of Serum Albumin Immobilized on Gold Nanoparticles

Ogunlusi

Driskell

2023

Langmuir

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Proteins adsorbed to gold nanoparticles (AuNPs) form bioconjugates and are critical to many emerging technologies for drug delivery, diagnostics, therapies, and other biomedical applications. A thorough understanding of the interaction between the immobilized protein and AuNP is essential for the bioconjugate to perform as designed. Here, we explore a correlation between the number of solvent-accessible thiol groups on a protein and the protein desorption rate from the AuNP surface in the presence of a competing protein. The chemical modification of human serum albumin (HSA) was carried out to install additional free thiols using Traut's reagent and create a library of HSA analogues by tailoring the molar excess of the Traut's reagent. We pre-adsorbed HSA variants onto the AuNP surface, and the resulting bioconjugates were then exposed to IgG antibody, and protein exchange was monitored as a function of time. We found that the rate of HSA displacement from the AuNP correlated with the experimentally measured number of accessible free thiol groups. Additionally, bioconjugates were synthesized using thiolated analogues of bovine serum albumin (BSA) and suspended in serum as a model for a complex sample matrix. Similarly, desorption rates with serum proteins were modulated with solvent-accessible thiols on the immobilized protein. These results further highlight the key role of Au−S bonds in the formation of protein−AuNP conjugates and provide a pathway to systematically control the number of free thiols on a protein, enabling the controlled release of protein from the surface of AuNP.

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Section: Results and Discussionmentioning

confidence: 98%

Controlled Temporal Release of Serum Albumin Immobilized on Gold Nanoparticles

Ogunlusi

Driskell

2023

Langmuir

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“…We further investigated how denaturation of HSA affects its binding to SRCR/CL region. It is worth noting that denaturation of HSA is quite common since the heating/chemical reactions of HSA solutions and the adsorption of HSA onto NP surface could alter the structure of HSA 56,57 . The procedure for generating the denatured HSA is described in the Methods section.…”

Section: Resultsmentioning

confidence: 99%

“…It is worth noting that denaturation of HSA is quite common since the heating/chemical reactions of HSA solutions and the adsorption of HSA onto NP surface could alter the structure of HSA. 56,57 The procedure for generating the denatured HSA is described in the Methods section. As shown in Figure 6A, there are significant structural differences between native and denatured HSA, with an RMSD greater than 11 Å. Additionally, the secondary structure is greatly altered, particularly the transformation from a helix to a coil/turn.…”

Section: Interaction Of Denatured Human Serum Albumin With Cl/srcr Re...mentioning

confidence: 99%

Effect of maleylation and denaturation of human serum albumin on its interaction with scavenger receptors

Yan

et al. 2023

Proteins

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The specific recognition of serum proteins by scavenger receptors is critical and fundamental in many biological processes. However, the underlying mechanism of scavenger receptor‐serum protein interaction remains elusive. In this work, taking scavenger receptors class A1 (SR‐A1) as an example, we systematically investigate its interaction with human serum albumin (HSA) at different states through a combination of molecular docking and all‐atom molecular dynamics simulations. It is found that native HSA can moderately bind to collagen‐like (CL) region or scavenger receptor cysteine‐rich (SRCR) region, with both electrostatic (ELE) and van der Waals (VDW) interactions, playing important roles. After maleylation, the binding energy, particularly the ELE energy, between HSA and CL region is significantly enhanced, while the binding energy between HSA and SRCR region remains nearly unchanged. Additionally, we also observe that unfolding of the secondary structures in HSA leads to a larger contact surface area between denatured HSA and CL region, but has little impact on the HSA‐SRCR region interaction. Therefore, similar to maleylated HSA, denatured HSA is also more likely to bind to the CL region of SR‐A1.

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Spontaneous desorption of protein from self-assembled monolayer (SAM)-coated gold nanoparticles induced by high temperature

Abstract: The nonspecific binding of protein with nanomaterial (NM) is a dynamic reversible process including both protein adsorption and desorption parts, which is crucial for controlled release of protein drug loaded...

Cited by 2 publications

References 63 publications

Controlled Temporal Release of Serum Albumin Immobilized on Gold Nanoparticles

Controlled Temporal Release of Serum Albumin Immobilized on Gold Nanoparticles

Effect of maleylation and denaturation of human serum albumin on its interaction with scavenger receptors

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