H-Bonding-mediated binding and charge reorganization of proteins on gold nanoparticles

Meesaragandla, Brahmaiah; Garcı́a, Isabel; Biedenweg, Doreen; Toro-Mendoza, Jhoan; Coluzza, Ivan; Liz‐Marzán, Luis M.; Delcea, Mihaela

doi:10.1039/c9cp06371d

Cited by 28 publications

(27 citation statements)

References 52 publications

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“…These polysaccharide coatings have been found to decrease the amount of proteins adsorbed on different types of materials, such as gold NPs (Henriksen‐lacey & Grzelczak, 2015) and carbon surfaces (Zen et al, 2016). Nevertheless, when compared to PEGylated particles, Meeseragandla et al found that glycan‐coated NPs adsorbed a greater amount of HSA molecules (Meesaragandla et al, 2020). These NP‐protein interactions were mostly attributed to the formation of hydrogen bonds, promoted by the presence of hydroxyl groups within the glycan structure, therefore questioning the efficiency of these ligands in preventing corona formation.…”

Section: Protein Corona As a Function Of Nanoparticle Surface Chemistrymentioning

confidence: 99%

Influence of surface chemistry and morphology of nanoparticles on protein corona formation

Bilardo

Traldi

Vdovchenko

et al. 2022

WIREs Nanomed Nanobiotechnol

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Nanomaterials offer promising solutions as drug delivery systems and imaging agents in response to the demand for better therapeutics and diagnostics. However, the limited understanding of the interaction between nanoparticles and biological entities is currently hampering the development of new systems and their applications in clinical settings. Proteins and lipids in biological fluids are known to complex with nanoparticles to form a "biomolecular corona". This has been shown to affect particles' morphology and behavior in biological systems and their interactions with cells. Hence, understanding how nanomaterials' physicochemical properties affect the formation and composition of this biocorona is a crucial step. This work evaluates existing literature on how morphology (size and shape), and surface chemistry (charge and hydrophobicity) of nanoparticles influence the formation of protein corona. The latest evidence suggest that although surface charge promotes the interaction with proteins and lipids, surface chemistry plays a leading role in determining the affinity of the nanoparticle for biomolecules and, ultimately, the composition of the corona. More recently the study of additional nanoparticles' properties like shape and surface chirality have demonstrated a significant effect on protein corona architecture, providing new tools to tailor biomolecular corona formation.

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Section: Protein Corona As a Function Of Nanoparticle Surface Chemistrymentioning

confidence: 99%

Influence of surface chemistry and morphology of nanoparticles on protein corona formation

Bilardo

Traldi

Vdovchenko

et al. 2022

WIREs Nanomed Nanobiotechnol

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“…Both Dex-10 and Cht-AuNPs show similar d H , even though the core size was different as shown in TEM images. This could be due to the multilayer adsorption of polymers on AuNPs surface 27,28 . Among all the biopolymer-coated AuNPs, a large increment in the d H was observed for the Dxt-AuNPs, which is due to the multilayer linear adsorption of Dxt molecules.…”

Section: Synthesis and Characterization Of Biopolymer-coated Aunps Bmentioning

confidence: 99%

Biopolymer-coated gold nanoparticles inhibit human insulin amyloid fibrillation

Meesaragandla

Karanth

Janke

et al. 2020

Sci Rep

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Deposits of protein misfolding and/or aggregates are a pathological hallmark of amyloid-related diseases. For instance, insulin amyloid fibril deposits have been observed in patients with insulindependent diabetes mellitus after insulin administration. Here, we report on the use of AuNPs functionalized with linear-(i.e. dextrin and chitosan) and branched-(i.e. dextran-40 and dextran-10) biopolymers as potential agents to inhibit insulin fibril formation. Our dynamic light scattering analyses showed a size decrease of the amyloid fibrils in the presence of functionalized AuNPs. Circular dichroism spectroscopy as well as enzyme-linked immunosorbent assay data demonstrated that the secondary structural transition from α-helix to β-sheet (which is characteristic for insulin amyloid fibril formation) was significantly suppressed by all biopolymer-coated AuNPs, and in particular, by those functionalized with linear biopolymers. Both transmission electron microscopy and atomic force microscopy analyses showed that the long thick amyloid fibrils formed by insulin alone become shorter, thinner or cluster when incubated with biopolymer-coated AuNPs. Dextrin-and chitosan-coated AuNPs were found to be the best inhibitors of the fibril formation. Based on these results, we propose a mechanism for the inhibition of insulin amyloid fibrils: biopolymer-coated AuNPsstrongly interact with the insulin monomers and inhibit the oligomer formation as well as elongation of the protofibrils.Moreover, cytotoxicity experiments showed that AuNP-insulin amyloid fibrils are less toxic compared to insulin amyloid fibrils alone. Our results suggest that both dextrin-and chitosan-AuNPs could be used as therapeutic agents for the treatment of amyloid-related disorders. Deposition of insoluble protein aggregates referred as amyloids has been observed as a common feature of various degenerative diseases (e.g. Alzheimer's, type II diabetes, Parkinson's, and Huntington's disease) 1-5. Almost 20 different human proteins have been identified to form amyloid deposits and aggregates in intracellular and extracellular matrix of the brain 6. Amyloid fibrils have been recognized as highly-ordered aggregates, rich in cross β-sheet secondary structures with unbranched filamentous morphology 7. Generally, amyloid fibril formation involves several steps including oligomers, protofibrils, and fibrils 8,9. Each of these forms has distinctive molecular conformations and different degrees of toxicity to the neuronal cells 10. One of the human proteins where amyloid fibril formation is considered a major problem is insulin. It is a 51-residue polypeptide hormone involved in regulating the blood glucose level and is used for the treatment of diabetes. It consists of an A-chain (21-residues) and B-chain (30-residues) which are connected by a pair of inter-chain disulfide bonds 11. Furthermore, it has been shown to exhibit an in vitro amyloid fibril-forming tendency at certain destabilizing conditions (e.g., low pH, elevated temperature, increased ionic strength, and ...

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“…Instead, these nano–bio interactions might be driven by other mechanisms, such as hydrogen bonding and hydrophobic interaction, as reported in previous works. [ 15 ]…”

Section: Resultsmentioning

confidence: 99%

Differential Macrophage Responses to Gold Nanostars and Their Implication for Cancer Immunotherapy

Kenry

Eschle

Andreiuk

et al. 2022

Advanced Therapeutics

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Gold nanostars (AuNSs) are actively explored for a range of theranostic and nanomedicine applications. While their biological applications are widely demonstrated, the fundamental interactions of these anisotropic nanomaterials with innate immune cells and their implication for cancer immunotherapy are less investigated. Specifically, it remains unclear how AuNSs interact with macrophages of different phenotypes and how these interactions influence the behavior of macrophages, especially their phagocytic and cancer modulating activities. Herein, the interactions between AuNSs of different shapes and macrophages of different phenotypes, including the naïve M0, pro‐inflammatory M1‐like, and anti‐inflammatory M2‐like phenotypes, are systematically interrogated. This study reveals that the morphology of AuNSs significantly impacts their interactions with macrophages. Macrophage viability, oxidative stress response, cytokine release, and phagocytotic ability depend on the macrophage phenotype as well as AuNS shape tip‐to‐core ratio. The selective response of macrophages toward AuNSs, particularly those of M1‐like phenotype, may be potentially leveraged for realizing cancer immunotherapy. Overall, it is anticipated that the findings of this study will further shape the understanding of the interactions between innate immune cells and Au nanomaterials and potentially open new opportunities for cancer therapy.

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H-Bonding-mediated binding and charge reorganization of proteins on gold nanoparticles

Abstract: Gold nanoparticles with various functionalities interact with the human serum albumin (HSA) leading to protein structural changes. HSA-nanoparticles bioconjugates display lower toxicity and slower cell uptake rates, compared to nanoparticles in the absence of protein.

Cited by 28 publications

References 52 publications

Influence of surface chemistry and morphology of nanoparticles on protein corona formation

Influence of surface chemistry and morphology of nanoparticles on protein corona formation

Biopolymer-coated gold nanoparticles inhibit human insulin amyloid fibrillation

Differential Macrophage Responses to Gold Nanostars and Their Implication for Cancer Immunotherapy

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