Las políticas y estrategias de China hacia América Latina y el Caribe

Niu, Haibin

doi:10.2307/j.ctv893gh5.7

Cited by 8 publications

(7 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…However, PI only crosses damaged cell membranes, intercalating with DNA forming a bright red fluorescent complex. 15 After treatment with PA 4 and PA 7, cells showed PI fluorescence, suggesting that their action involves permeation of the microorganism's membrane, similar to other AMPs (Figure 4 and S8). 10 The incorporation of PI in S. aureus and E. coli K12 treated with PAs was further evaluated by flow cytometry.…”

Section: Pa Amphiphile Micelles Action On Bacteria Membranementioning

confidence: 71%

Design, Synthesis, and Nanostructure-Dependent Antibacterial Activity of Cationic Peptide Amphiphiles

Almeida

Han

Perez

et al. 2018

ACS Appl. Mater. Interfaces

112

View full text Add to dashboard Cite

The development of bacterial resistant strains is a global health concern. Designing antibiotics that limit the rise of pathogenic resistance is essential to efficiently treat pathogenic infections. Selfassembling amphiphilic molecules are an intriguing platform for the treatment of pathogens due to their ability to disrupt bacterial membranes and function as drug nanocarriers. We have designed cationic peptide amphiphiles (PAs) that can form micelles, nanofibers, and twisted ribbons with the aim of understanding antimicrobial activity at the supramolecular level. We have found that micelle-forming PAs possess excellent antimicrobial activity against various Gram-positive and Gram-negative pathogens, such as methicillin-resistant S. aureus and multidrug resistant K. pneumoniae with MICs ranging between 1-8 µg/mL when compared to nanofibers with MICs >32 µg/mL. The data suggest the antimicrobial activity of the PAs depends on their morphology, amino-acids sequence, the length of the alkyl tail, and the overall hydrophobicity of the PA. Scanning electron microscopy, confocal microscopy, and flow cytometry studies using MRSA and E. coli K12 strains showed that PAs increase cell membrane permeability, and disrupt the integrity of the pathogen's membrane, leading to cell lysis and death. PAs are a promising platform to develop new antimicrobials that could work as nanocarriers to develop synergistic antibacterial therapies.

show abstract

Section: Pa Amphiphile Micelles Action On Bacteria Membranementioning

confidence: 71%

Design, Synthesis, and Nanostructure-Dependent Antibacterial Activity of Cationic Peptide Amphiphiles

Almeida

Han

Perez

et al. 2018

ACS Appl. Mater. Interfaces

112

View full text Add to dashboard Cite

show abstract

“…The interstitial spaces in the shell were utilized to load antibodies. 82 Building on this, RSNs were designed with controlled surface roughness and longer neck space by complexing larger anionic SiNPs as the shell on amine-modified cores. 83 These anionic RSNs were loaded with positively charged anti-phospho-Akt via electrostatic complexation, which showed successful release in human breast cancer (MCF-7) cells.…”

Section: Inorganic Nanoparticlesmentioning

confidence: 99%

“…82 Building on this, RSNs were designed with controlled surface roughness and longer neck space by complexing larger anionic SiNPs as the shell on amine-modified cores. 83 These anionic RSNs were loaded with positively charged anti-phospho-Akt via electrostatic complexation, which showed successful release in human breast cancer (MCF-7) cells. In a follow up work, it was found that the enhanced surface roughness and void sizes determine high loading ability, while a hydrophobic octadecyl (C18) functionality plays a key role in better uptake via endocytosis and endo/lysosomal escape of RSNs.…”

Section: Inorganic Nanoparticlesmentioning

confidence: 99%

“…In a follow up work, it was found that the enhanced surface roughness and void sizes determine high loading ability, while a hydrophobic octadecyl (C18) functionality plays a key role in better uptake via endocytosis and endo/lysosomal escape of RSNs. 84 Similarly, a therapeutic antibody Cetuximab was encapsulated in a biodegradable silica nanoquencher (BS-qNP), which was shown to be efficiently taken up by cancer cells and underwent degradation in the presence of the hypoxic environment specific to cancer cells 85 (Fig. 5).…”

Section: Inorganic Nanoparticlesmentioning

confidence: 99%

See 1 more Smart Citation

Antibody Delivery for Intracellular Targets: Emergent Therapeutic Potential

et al. 2019

View full text Add to dashboard Cite

Proteins have sparked fast growing interest as biological therapeutic agents for several diseases. Antibodies, in particular, carry an enormous potential as drugs owing to their remarkable target specificity and low immunogenicity. Although the market has numerous antibodies directed towards extracellular targets, their use in targeting therapeutically important intracellular targets is limited by their inability to cross cellular membrane. Realizing the potential for antibody therapy in disease treatment, progress has been made in the development of methods to deliver antibodies intracellularly. In this review, we address various platforms for delivery of antibodies, their merits and drawbacks.

show abstract

“…13 We use the anti-amylin polyclonal antibody (Thermo Fisher Scientific, PA1-37075), which is derived from rabbit anti-IgG and raised against the N-terminal sequence of synthetic hIAPP. The antibody is incubated in the presence of CS 2 in deuterated phosate buffered saline (PBS, Fisher Scientific, pH 7.4) for 24 h to chemically link the amine side chains of the lysine residues to the gold surface, 33,34 as shown in Figure 1a,b. The CS 2 reacts with the amine groups, and the thiol links the antibodies to the gold before being rinsed three times with PBS.…”

mentioning

confidence: 99%

Monolayer Sensitivity Enables a 2D IR Spectroscopic Immuno-biosensor for Studying Protein Structures: Application to Amyloid Polymorphs

Ostrander

Lomont

Rich

et al. 2019

J. Phys. Chem. Lett.

View full text Add to dashboard Cite

Immunosensors use antibodies to detect and quantify biomarkers of disease, though the sensors often lack structural information. We create a surface-sensitive two-dimensional infrared (2D IR) spectroscopic immunosensor for studying protein structures. We tether antibodies to a plasmonic surface, flow over a solution of amyloid proteins, and measure the 2D IR spectra. The 2D IR spectra provide a global assessment of antigen structure, and isotopically labeled proteins give residue-specific structural information. We report the 2D IR spectra of fibrils and monomers using a polyclonal antibody that targets human islet amyloid polypeptide (hIAPP). We observe two fibrillar polymorphs differing in their structure at the G24 residue, which supports the hypothesis that hIAPP polymorphs form from a common oligomeric intermediate. This work provides insight into the structure of hIAPP, establishes a new method for studying protein structures using 2D IR spectroscopy, and creates a spectroscopic immunoassay applicable for studying a wide range of biomarkers.

show abstract

Las políticas y estrategias de China hacia América Latina y el Caribe

Cited by 8 publications

References 0 publications

Design, Synthesis, and Nanostructure-Dependent Antibacterial Activity of Cationic Peptide Amphiphiles

Design, Synthesis, and Nanostructure-Dependent Antibacterial Activity of Cationic Peptide Amphiphiles

Antibody Delivery for Intracellular Targets: Emergent Therapeutic Potential

Monolayer Sensitivity Enables a 2D IR Spectroscopic Immuno-biosensor for Studying Protein Structures: Application to Amyloid Polymorphs

Contact Info

Product

Resources

About