Using the dendritic polymer PAMAM to form gold nanoparticles in the protein cage thermosome

Many protein cages, including the chaperonin thermosome (THS), lack the ability to form inorganic nanoparticles. By conjugation of PAMAM into THS, metal ions could bind to the dendrimer and allowed the formation of gold nanoparticles in the protein cage.

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Polyelectrolyte Encapsulation and Confinement within Protein Cage-Inspired Nanocompartments

Pharmaceutics ◽

10.3390/pharmaceutics13101551 ◽

2021 ◽

Vol 13 (10) ◽

pp. 1551

Author(s):

Qing Liu ◽

Ahmed Shaukat ◽

Daniella Kyllönen ◽

Mauri A. Kostiainen

Keyword(s):

Small Molecules ◽

Driving Force ◽

Electrostatic Interactions ◽

Inorganic Nanoparticles ◽

Wild Type ◽

Potential Toxicity ◽

Protein Cages ◽

Functional Sites ◽

Protein Cage ◽

Or Gene

Protein cages are nanocompartments with a well-defined structure and monodisperse size. They are composed of several individual subunits and can be categorized as viral and non-viral protein cages. Native viral cages often exhibit a cationic interior, which binds the anionic nucleic acid genome through electrostatic interactions leading to efficient encapsulation. Non-viral cages can carry various cargo, ranging from small molecules to inorganic nanoparticles. Both cage types can be functionalized at targeted locations through genetic engineering or chemical modification to entrap materials through interactions that are inaccessible to wild-type cages. Moreover, the limited number of constitutional subunits ease the modification efforts, because a single modification on the subunit can lead to multiple functional sites on the cage surface. Increasing efforts have also been dedicated to the assembly of protein cage-mimicking structures or templated protein coatings. This review focuses on native and modified protein cages that have been used to encapsulate and package polyelectrolyte cargos and on the electrostatic interactions that are the driving force for the assembly of such structures. Selective encapsulation can protect the payload from the surroundings, shield the potential toxicity or even enhance the intended performance of the payload, which is appealing in drug or gene delivery and imaging.

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Green Synthesis of Silver and Gold Nanoparticles via Sargassum serratifolium Extract for Catalytic Reduction of Organic Dyes

Catalysts ◽

10.3390/catal11030347 ◽

2021 ◽

Vol 11 (3) ◽

pp. 347

Author(s):

Beomjin Kim ◽

Woo Chang Song ◽

Sun Young Park ◽

Geuntae Park

Keyword(s):

Gold Nanoparticles ◽

Green Synthesis ◽

Catalytic Reduction ◽

Organic Dyes ◽

Low Cost ◽

Inorganic Nanoparticles ◽

X Ray ◽

Selected Area Electron Diffraction ◽

Transmission Electron ◽

Sargassum Serratifolium

The green synthesis of inorganic nanoparticles (NPs) using bio-materials has attained enormous attention in recent years due to its simple, eco-friendly, low-cost and non-toxic nature. In this work, silver nanoparticles (AgNPs) and gold nanoparticles (AuNPs) were synthesized by the marine algae extract, Sargassum serratifolium (SS). The characteristic studies of bio-synthesized SS-AgNPs and SS-AuNPs were carried out by using ultraviolet–visible (UV–Vis) absorption spectroscopy, dynamic light scattering (DLS), high-resolution transmission electron microscope (HR-TEM), selected area electron diffraction (SAED), energy-dispersive X-ray spectroscopy (EDX), X-ray powder diffraction (XRD) and Fourier transform infrared spectroscopy (FT-IR). Phytochemicals in the algae extract, such as meroterpenoids, acted as a capping agent for the NPs’ growth. The synthesized Ag and Au NPs were found to have important catalytic activity for the degradation of organic dyes, including methylene blue, rhodamine B and methyl orange. The reduction of dyes by SS-AgNPs and -AuNPs followed the pseudo-first order kinetics.

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Colorimetric Detection of Toxic Metal Ions in Water on the Basis of Gold Nanoparticles

Nanomaterials for Water Management ◽

10.1201/b18715-6 ◽

2015 ◽

pp. 71-102

Keyword(s):

Gold Nanoparticles ◽

Metal Ions ◽

Colorimetric Detection ◽

Toxic Metal ◽

Toxic Metal Ions

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Laboratory evolution of virus-like nucleocapsids from nonviral protein cages

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1800527115 ◽

2018 ◽

Vol 115 (21) ◽

pp. 5432-5437 ◽

Cited By ~ 17

Author(s):

Naohiro Terasaka ◽

Yusuke Azuma ◽

Donald Hilvert

Keyword(s):

Aquifex Aeolicus ◽

Cellular Functions ◽

Laboratory Evolution ◽

Virion Assembly ◽

Protein Cages ◽

Protein Cage ◽

Spherical Structures ◽

Rna Genome ◽

Biological Environment

Viruses are remarkable nanomachines that efficiently hijack cellular functions to replicate and self-assemble their components within a complex biological environment. As all steps of the viral life cycle depend on formation of a protective proteinaceous shell that packages the DNA or RNA genome, bottom-up construction of virus-like nucleocapsids from nonviral materials could provide valuable insights into virion assembly and evolution. Such constructs could also serve as safe alternatives to natural viruses for diverse nano- and biotechnological applications. Here we show that artificial virus-like nucleocapsids can be generated—rapidly and surprisingly easily—by engineering and laboratory evolution of a nonviral protein cage formed by Aquifex aeolicus lumazine synthase (AaLS) and its encoding mRNA. Cationic peptides were appended to the engineered capsid proteins to enable specific recognition of packaging signals on cognate mRNAs, and subsequent evolutionary optimization afforded nucleocapsids with expanded spherical structures that encapsulate their own full-length RNA genome in vivo and protect the cargo molecules from nucleases. These findings provide strong experimental support for the hypothesis that subcellular protein-bounded compartments may have facilitated the emergence of ancient viruses.

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