Influence of ligands property and particle size of gold nanoparticles on the protein adsorption and corresponding targeting ability

Xiao, Wei; Xiong, Jingyuan; Zhang, Shuang; Xiong, Yang; Zhang, Huajin; Gao, Huile

doi:10.1016/j.ijpharm.2018.01.011

Cited by 93 publications

(46 citation statements)

References 52 publications

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“…Our results can explain the contradictions in data obtained on PEG-functionalized AuNPs. Seemingly, these contradictions can be explained by a different degree in PEG functionalization as well as the size of PEG groups attached [26,27,30,31,41]. Thus, functionalization of AuNP by carbosilane dendrons can be useful in preventing their interaction with serum proteins.…”

Section: Discussionmentioning

confidence: 99%

“…In contrast, Prasanth et al [29] after spectroscopic analysis of interaction between PEGfunctionalized Ag 2 S nanoparticles with bovine serum albumin concluded that the overall conformation of BSA is unaltered after complexation with PEG-functionalized Ag 2 S nanoparticles and hence BSA is expected to be functional. Also, Xiao et al [30] reported that the preliminary adsorption of PEG by nanoparticles can significantly avoid the adsorption of plasma proteins. Joshi et al [31] found that binding of chloroquine-conjugated gold nanoparticles with bovine serum albumin is accompanied with only a minor alteration in the protein structure.…”

Section: Introductionmentioning

confidence: 99%

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Role of cationic carbosilane dendrons and metallic core of functionalized gold nanoparticles in their interaction with human serum albumin

Shcharbin

Pedziwiatr-Werbicka

Serchenya

et al. 2018

International Journal of Biological Macromolecules

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Functionalization of gold nanoparticles by different chemical groups is an important issue regarding the biomedical applications of such particles. Therefore we have analyzed the interaction between gold nanoparticles functionalized by carbosilane dendrons with human serum albumin at different pHs, and in the presence of the protein unfolding agent, guanidine hydrochloride, using circular dichroism, zeta-potential and fluorescence quenching. The effect of a nanoparticle dendronization and pure dendrons on the immunoreactivity of albumin was estimated using ELISA. In addition, the tool to estimate the binding capacity of dendronized gold nanoparticles using a hydrophobic fluorescent probe 1,8-ANS (1-anilinonaphthalene-8-sulfonic acid) was chosen. We concluded that the effect of a nanoparticle on the structure, immunochemical properties and unfolding of albumin significantly decreased with second and third generations dendrons attached. Differences in pH dependence of the interaction between nanoparticles, their dendrons and albumin showed several effects of the "dendritic corona" and the metallic part of nanoparticle on the protein. These interactions indicate changes in the immunoreactivity of the protein, whereas dendron coating per se had no effect. Thus, dendronization of gold nanoparticles helps to shield them from interactions with plasma proteins.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Role of cationic carbosilane dendrons and metallic core of functionalized gold nanoparticles in their interaction with human serum albumin

Shcharbin

Pedziwiatr-Werbicka

Serchenya

et al. 2018

International Journal of Biological Macromolecules

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“…In addition, the formed PC shows different effects on the targeting ability of different target molecules. [ 72 ] The targeting abilities of c(RGDyC) (RGD) peptide and transferrin (Tf) were comparatively studied in the presence of the PC. RGD showed a better targeting effect than Tf without the PC, but after plasma proteins adsorption, Tf‐GNPs demonstrated a higher targeting ability than RGD‐GNPs.…”

Section: Pc‐modulated Biodistribution and Tumor‐targeting Of Gnpsmentioning

confidence: 99%

Biological Behavior Regulation of Gold Nanoparticles via the Protein Corona

Hong

Ding

2020

Adv Healthcare Materials

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One of the difficulties in the translation of gold nanoparticles (GNPs) into clinical practice is the formation of the protein corona (PC) that causes the discrepancy between the in vitro and in vivo performance of GNPs. The PC formed on the surface of GNPs gives them a biological identity instead of an initial synthetic one. In most instances, this biological identity increases the particle size, leads to more clearance by the reticuloendothelial system, and causes less uptake by target cells. However, the performance of GNPs can still be improved by rewriting their original surface chemistry via the PC. This review specifically focuses on discussing the main influence factors, including the biological environment and physicochemical properties of GNPs, which affect the production and status of the PC. The status of the PC such as the amount, thickness, and composition subsequently influence the biological behavior of GNPs, especially their cellular uptake, cytotoxicity, biodistribution, and tumor targeting. Further understanding and revealing the impacts of the PC on the biological behavior of GNPs can be a promising and important strategy to regulate and improve the performance of GNP‐based biosystems in the future.

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“…Currently, the design of anticancer therapeutics is focused on creating new systems with low toxicity, e.g., those based on nanocarriers, enabling targeted delivery and high efficiency of the treatment [1]. Usually, it is assumed that immediately after being introduced into the blood, nanoparticles (NPs) are surrounded by plasma proteins that form a biological coating around the individual NPs, known as the protein corona [1][2][3][4][5][6][7][8][9][10]. Various characteristics of NPs (their size and shape, surface properties, etc.)…”

Section: Introductionmentioning

confidence: 99%

“…have an influence on a formation mechanism of the protein corona [5,7]. In this respect, two categories of proteins can be distinguished: opsonins, which can increase the recognition of the reticuloendothelial system and, as a result, lead to a rapid elimination from the organism, and dysopsonins, which can improve the blood circulation time of NPs [9][10][11]. Therefore, when creating targeted drug delivery systems (DDS), knowledge about the protein-NP interaction mechanism can be crucial.…”

Section: Introductionmentioning

confidence: 99%

Molecular Mechanisms of the Interactions of N-(2-Hydroxypropyl)methacrylamide Copolymers Designed for Cancer Therapy with Blood Plasma Proteins

et al. 2020

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The binding of plasma proteins to a drug carrier alters the circulation of nanoparticles (NPs) in the bloodstream, and, as a consequence, the anticancer efficiency of the entire nanoparticle drug delivery system. We investigate the possible interaction and the interaction mechanism of a polymeric drug delivery system based on N-(2-hydroxypropyl)methacrylamide (HPMA) copolymers (pHPMA) with the most abundant proteins in human blood plasma—namely, human serum albumin (HSA), immunoglobulin G (IgG), fibrinogen (Fbg), and apolipoprotein (Apo) E4 and A1—using a combination of small-angle X-ray scattering (SAXS), analytical ultracentrifugation (AUC), and nuclear magnetic resonance (NMR). Through rigorous investigation, we present evidence of weak interactions between proteins and polymeric nanomedicine. Such interactions do not result in the formation of the protein corona and do not affect the efficiency of the drug delivery.

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Influence of ligands property and particle size of gold nanoparticles on the protein adsorption and corresponding targeting ability

Cited by 93 publications

References 52 publications

Role of cationic carbosilane dendrons and metallic core of functionalized gold nanoparticles in their interaction with human serum albumin

Role of cationic carbosilane dendrons and metallic core of functionalized gold nanoparticles in their interaction with human serum albumin

Biological Behavior Regulation of Gold Nanoparticles via the Protein Corona

Molecular Mechanisms of the Interactions of N-(2-Hydroxypropyl)methacrylamide Copolymers Designed for Cancer Therapy with Blood Plasma Proteins

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