Unveiling the interaction of protein fibrils with gold nanoparticles by plasmon enhanced nano-spectroscopy

Capocefalo, Angela; Deckert‐Gaudig, Tanja; Brasili, Francesco; Postorino, P.; Deckert, Volker

doi:10.1039/d1nr03190b

Cited by 10 publications

(8 citation statements)

References 76 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our findings can be also compared with the disassembling effect of functionalized metallic (gold and silver) nanoparticles on the lysozyme amyloid fibrils studied previously [ 75 , 76 , 77 ], and also attributed to their electrostatic interactions with the protein. Negatively charged silver and iron nanoparticles were reported to sequester monomers of the positively charged human islet amyloid polypeptide and inhibit fibril formation [ 78 ].…”

Section: Discussionsupporting

confidence: 53%

The Ability of Some Polysaccharides to Disaggregate Lysozyme Amyloid Fibrils and Renature the Protein

et al. 2023

View full text Add to dashboard Cite

The deposition of proteins in the form of insoluble amyloid fibril aggregates is linked to a range of diseases. The supramolecular architecture of such deposits is governed by the propagation of β-strands in the direction of protofilament growth. In the present study, we analyze the structural changes of hen egg-white lysozyme fibrils upon their interactions with a range of polysaccharides, using AFM and FTIR spectroscopy. Linear anionic polysaccharides, such as κ-carrageenan and sodium alginate, are shown to be capable to disaggregate protofilaments with eventual protein renaturation. The results help to understand the mechanism of amyloid disaggregation and create a platform for both the development of new therapeutic agents for amyloidose treatment, and the design of novel functional protein–polysaccharide complex-based nanomaterials.

show abstract

Section: Discussionsupporting

confidence: 53%

The Ability of Some Polysaccharides to Disaggregate Lysozyme Amyloid Fibrils and Renature the Protein

et al. 2023

View full text Add to dashboard Cite

show abstract

“…In TERS, the illumination can occur in different forms shown in Figure 1d. The spectra obtained from SERS and TERS (Figure 1b) are markedly different from NR due to the probed areas (Capocefalo et al, 2021;Kurouski et al, 2012Kurouski et al, , 2013. The detailed interpretation of the vibrational spectra of proteins and their aggregates is discussed in the sections below.…”

Section: Working Principles Of Raman and Its Plasmon-enhanced Variantsmentioning

confidence: 97%

“…Surface‐enhanced Raman spectroscopy (SERS) is a variant of plasmon‐enhanced Raman spectroscopy (PERS) to probe the surface of macromolecules and other biological entities with high sensitivity and selectivity (Chen et al, 2016; Singh et al, 2022; D. M. Zhang et al, 2009; Zhou et al, 2020). For studying protein aggregation, SERS can be combined with SPM to probe the structural organization and its corresponding chemical constituents at the nanoscale level, which has been demonstrated in the case of insulin fibrils (Capocefalo et al, 2021; Groenning et al, 2009). This unique integrated technique known as tip‐enhanced Raman spectroscopy (TERS) enables the study of the topology and the secondary structural components of proteins, along with the spatial organization of amino acids on the surfaces of proteins.…”

Section: Introductionmentioning

confidence: 99%

Raman spectroscopy and its plasmon‐enhanced counterparts: A toolbox to probe protein dynamics and aggregation

Dhillon

Sharma

Yadav

et al. 2023

WIREs Nanomed Nanobiotechnol

View full text Add to dashboard Cite

Protein unfolding and aggregation are often correlated with numerous diseases such as Alzheimer's, Parkinson's, Huntington's, and other debilitating neurological disorders. Such adverse events consist of a plethora of competing mechanisms, particularly interactions that control the stability and cooperativity of the process. However, it remains challenging to probe the molecular mechanism of protein dynamics such as aggregation, and monitor them in real‐time under physiological conditions. Recently, Raman spectroscopy and its plasmon‐enhanced counterparts, such as surface‐enhanced Raman spectroscopy (SERS) and tip‐enhanced Raman spectroscopy (TERS), have emerged as sensitive analytical tools that have the potential to perform molecular studies of functional groups and are showing significant promise in probing events related to protein aggregation. We summarize the fundamental working principles of Raman, SERS, and TERS as nondestructive, easy‐to‐perform, and fast tools for probing protein dynamics and aggregation. Finally, we highlight the utility of these techniques for the analysis of vibrational spectra of aggregation of proteins from various sources such as tissues, pathogens, food, biopharmaceuticals, and lastly, biological fouling to retrieve precise chemical information, which can be potentially translated to practical applications and point‐of‐care (PoC) devices.This article is categorized under: Therapeutic Approaches and Drug Discovery > Emerging Technologies Diagnostic Tools > Diagnostic Nanodevices Nanotechnology Approaches to Biology > Nanoscale Systems in Biology

show abstract

“…Nanomaterials such as gold, silver, copper, selenium, titanium, zinc oxide, and magnesium oxide have antimicrobial activity against human pathogenic bacteria and fungi [ 18 , 19 , 20 , 21 ]. Among them, gold nanoparticles are considered one of the most commonly used metals for biomedical applications due to their unique properties, such as adjustable size, shape, surface properties, optical properties, biocompatibility, low cytotoxicity, and high stability [ 22 , 23 , 24 ]. In the majority of nanomaterials described in recent studies, antibacterial activity is attributed to at least one of the following mechanisms: inhibition of cell wall/membrane synthesis, disruption of energy conversion, production of toxic reactive oxygen species (ROS), photocatalysis, enzyme inhibition, and reduction of DNA production [ 25 , 26 ].…”

Section: Introductionmentioning

confidence: 99%

Synthesis of Chitosan-Based Gold Nanoparticles: Antimicrobial and Wound-Healing Activities

et al. 2022

View full text Add to dashboard Cite

The global spread of multidrug-resistant bacteria has become a significant hazard to public health, and more effective antibacterial agents are required. Therefore, this study describes the preparation, characterization, and evaluation of gold nanoparticles modified with chitosan (Chi/AuNPs) as a reducing and stabilizing agent with efficient antimicrobial effects. In recent years, the development of an efficient and ecofriendly method for synthesizing metal nanoparticles has attracted a lot of interest in the field of nanotechnology. Colloidal gold nanoparticles (AuNPs) were prepared by the chemical reduction of gold ions in the presence of chitosan (Chi), giving Chi/AuNPs. The characterization of Chi/AuNPs was carried out by transmission electron microscopy (TEM), scanning electron microscopy (SEM), Fourier-transform infrared (FTIR), and X-ray diffraction (XRD). Chi/AuNPs appeared spherical and monodispersed, with a diameter ranging between 20 to 120 nm. The synergistic effects of AuNPs and Chi led to the disruption of bacterial membranes. The maximum inhibitory impact was seen against P. aeruginosa at 500 µg/mL, with a zone of inhibition diameter of 26 ± 1.8 mm, whereas the least inhibitory effect was reported for S. aureus, with a zone of inhibition diameter of 16 ± 2.1 mm at the highest dose tested. Moreover, Chi/AuNPs exhibited antifungal activity toward Candida albicans when the MIC was 62.5 µg/mL. Cell viability and proliferation of the developed nanocomposite were evaluated using a sulphorhodamine B (SRB) assay with a half inhibitory concentration (IC50) of 111.1 µg/mL. Moreover, the in vitro wound-healing model revealed that the Chi/AuNP dressing provides a relatively rapid and efficacious wound-healing ability, making the obtained nanocomposite a promising candidate for the development of improved bandage materials.

show abstract

Unveiling the interaction of protein fibrils with gold nanoparticles by plasmon enhanced nano-spectroscopy

Abstract: The development of various degenerative diseases is suggested to be triggered by the uncontrolled organisation and aggregation of proteins into amyloid fibrils. For this reason, there are ongoing efforts to...

Cited by 10 publications

References 76 publications

The Ability of Some Polysaccharides to Disaggregate Lysozyme Amyloid Fibrils and Renature the Protein

The Ability of Some Polysaccharides to Disaggregate Lysozyme Amyloid Fibrils and Renature the Protein

Raman spectroscopy and its plasmon‐enhanced counterparts: A toolbox to probe protein dynamics and aggregation

Synthesis of Chitosan-Based Gold Nanoparticles: Antimicrobial and Wound-Healing Activities

Contact Info

Product

Resources

About