Photo-synthesis of protein-based nanoparticles and the application in drug delivery

Xie, Jianping; Wang, Hongyang; Cao, Yi; Qin, Meng; Wang, Wei

doi:10.1016/j.aop.2015.03.029

Cited by 7 publications

(5 citation statements)

References 80 publications

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“…Thus, based on these similarities, we attribute the 150 ns and 2.0 ms components to the decay kinetics of Trp + and RSSR À , respectively. Although Tyr has also been shown to be able to promote disulfide bond cleavage, 45,46 it is unlikely that in the current case the single Tyr residue in Trp-Z34C is responsible for the observed kinetics because it is several residues away from the disulfide bond and its absorbance at the excitation wavelength is approximately an order of magnitude lower than that of the two Trp residues.…”

Section: Resultsmentioning

confidence: 75%

Direct measurement of the tryptophan-mediated photocleavage kinetics of a protein disulfide bond

Abaskharon

Gai

2016

Phys. Chem. Chem. Phys.

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Disulfide cleavage is one of the major causes underlying ultraviolet (UV) light-induced protein damages. While previous studies have provided strong evidence to support the notion that this process is mediated by photo-induced electron transfer from the excited state of an aromatic residue (e.g., tryptophan) to the disulfide bond, many mechanistic details are still lacking. For example, we do not know how quickly this process occurs in a protein environment. Herein, we design an experiment, which uses the unfolding kinetics of a protein as an observable, to directly assess the kinetics and mechanism of photo-induced disulfide cleavage. Our results show that this disulfide bond cleavage event takes place in ∼2 μs via a mechanism involving electron transfer from the triplet state of a tryptophan (Trp) residue to the disulfide bond. Furthermore, we find that one of the photoproducts of this reaction, a Trp-SR adduct, is formed locally, thus preventing the protein from re-cross-linking. Taken together, these findings suggest that a Trp-disulfide pair could be used as a photo-trigger to initiate protein folding dynamics and to control biological activities of disulfide-containing peptides.

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Section: Resultsmentioning

confidence: 75%

Direct measurement of the tryptophan-mediated photocleavage kinetics of a protein disulfide bond

Abaskharon

Gai

2016

Phys. Chem. Chem. Phys.

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“…Combinational strategies (e.g., complexes and covalent hybrids of different nanomaterials) for the design of nanovectors have received wide attention, including combinations of liposomes and polymers, polymers and inorganic nano-particles, and inorganic nanoparticle-peptide-polymers. [122][123][124][125][126] These synthesized composite carriers combine the advantages of multiple vectors, and produce improved siRNA transmission and gene silencing when compared with single type nanocarriers, suggesting that this is likely the best approach to future research on siRNA carriers and the broader impact of RNAi technology and nanomaterials on clinical applications.…”

Section: Conclusion and Prospectsmentioning

confidence: 99%

Powering up the molecular therapy of RNA interference by novel nanoparticles

Liao

Li²,

Zhang

et al. 2016

Biomater. Sci.

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RNA interference technology has been widely applied in biomedical therapy in recent years. A type of small RNA molecule - siRNA could regulate the expression of disease related genes by breaking down the integrity of mRNA with high specificity. However, the low efficiency of siRNA delivery to its target seriously hampered the RNAi therapy. Compared with viral-based delivery systems, non-viral-based nanoparticles are more suitable for disease treatment due to reduced cellular toxicity, higher loading capacity, and better biocompatibility. This review article highlights several nanoparticle-based siRNA delivery systems, including liposomes, cationic solid lipid nanoparticles, reconstituted high density lipoprotein, polymeric nanoparticles, cationic cell penetrating peptides, and inorganic nanoparticles. The molecular mechanism of gene silencing, clinical examples, and the limitations of current technology related to nanomaterial sciences, are also discussed.

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“…Irradiating proteins by UV light is proven to be a simple method for producing thiol groups from disulfide bonds. [33] Under a UV-intensity of 2 mW cm À 2 , lysozyme quickly produced new thiol groups and self-assembled into nanoparticles due to the exposure of hydrophobic regions. [34] The size of the resulting nanoparticles was controlled by changing the irradiation time and surface modification of PEG chains.…”

Section: Loading Of Drugs By Self-assembled Protein Nanoparticlesmentioning

confidence: 99%

“…Methods without the need of addition of reducing agents have been explored to stabilize protein nanoparticles. Irradiating proteins by UV light is proven to be a simple method for producing thiol groups from disulfide bonds . Under a UV‐intensity of 2 mW cm −2 , lysozyme quickly produced new thiol groups and self‐assembled into nanoparticles due to the exposure of hydrophobic regions .…”

Section: Introductionmentioning

confidence: 99%

Self‐Assembling Proteins for Design of Anticancer Nanodrugs

Zou

Chang

Yan

2020

Chemistry An Asian Journal

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Inspired by the diverse protein-based structures and materials in organisms, proteins have been expected as promising biological components for constructing nanomaterials toward various applications. In numerous studies protein-based nanomaterials have been constructed with the merits of abundant bioactivity and good biocompatibility. However, self-assembly of proteins as a dominant approach in constructing anticancer nanodrugs has not been reviewed.Here, we provide a comprehensive account of the role of protein self-assembly in fabrication, regulation, and application of anticancer nanodrugs. The supramolecular strategies, building blocks, and molecular interactions of protein selfassembly as well as the properties, functions, and applica-tions of the resulting nanodrugs are discussed. The applications in chemotherapy, radiotherapy, photodynamic therapy, photothermal therapy, gene therapy, and combination therapy are included. Especially, manipulation of molecular interactions for realizing cancer-specific response and cancer theranostics are emphasized. By expounding the impact of molecular interactions on therapeutic activity, rational design of highly efficient protein-based nanodrugs for precision anticancer therapy can be envisioned. Also, the challenges and perspectives in constructing nanodrugs based on protein self-assembly are presented to advance clinical translation of protein-based nanodrugs and next-generation nanomedicine. 2 3 4 5 6 7 8

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Photo-synthesis of protein-based nanoparticles and the application in drug delivery

Cited by 7 publications

References 80 publications

Direct measurement of the tryptophan-mediated photocleavage kinetics of a protein disulfide bond

Direct measurement of the tryptophan-mediated photocleavage kinetics of a protein disulfide bond

Powering up the molecular therapy of RNA interference by novel nanoparticles

Self‐Assembling Proteins for Design of Anticancer Nanodrugs

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