scholarly journals Aggregation kinetics and cluster structure of amino-PEG covered gold nanoparticles

RSC Advances ◽  
2016 ◽  
Vol 6 (32) ◽  
pp. 27151-27157 ◽  
Author(s):  
D. Zámbó ◽  
Sz. Pothorszky ◽  
D. F. Brougham ◽  
A. Deák
Keyword(s):  
Gold Nanoparticles ◽  
Self Assembly ◽  
Cluster Structure ◽  
Aggregation Kinetics ◽  
Kinetics Of

Perturbation induced directed self-assembly of amino PEGylated gold nanoparticles: kinetics of aggregation and cluster structure.

Aggregation Kinetics of Gold Nanoparticles at the Silica−Water Interface

2009 ◽  
Vol 113 (14) ◽  
pp. 5514-5519 ◽  
Author(s):  
Ivo K. J. Kretzers ◽  
Robert J. Parker ◽  
Rouslan V. Olkhov ◽  
Andrew M. Shaw
Keyword(s):  
Gold Nanoparticles ◽  
Aggregation Kinetics ◽  
Water Interface ◽  
Kinetics Of

The effect of temperature on the aggregation kinetics of partially bare gold nanoparticles

RSC Advances ◽  
2016 ◽  
Vol 6 (85) ◽  
pp. 82138-82149 ◽  
Author(s):  
Anushree Dutta ◽  
Anumita Paul ◽  
Arun Chattopadhyay
Keyword(s):  
Activation Energy ◽  
Gold Nanoparticles ◽  
Effect Of Temperature ◽  
Aggregation Kinetics ◽  
Temperature Dependent ◽  
Colloidal Aggregation ◽  
First Order ◽  
First Order Kinetics ◽  
Kinetics Of ◽  
Bare Gold

Temperature dependent aggregation reaction of partially bare gold nanoparticles showed a first order kinetics and prevalence of reaction limited colloidal aggregation with an activation energy equal to 36.2 ± 3.0 kJ mol−1.

scholarly journals Nucleation-dependent aggregation kinetics of Yeast Sup35 fragment GNNQQNY

2020 ◽  
Author(s):  
Gunasekhar Burra ◽  
Mahmoud B. Maina ◽  
Louise C. Serpell ◽  
Ashwani K. Thakur
Keyword(s):  
Self Assembly ◽  
Amyloid Fibrils ◽  
Peptide Sequence ◽  
Aggregation Kinetics ◽  
Assembly Mechanism ◽  
Structural Identity ◽  
Different Temperatures ◽  
Dynamics Simulations ◽  
Amyloid Assembly ◽  
Kinetics Of

AbstractAn N-terminal hepta-peptide sequence of yeast prion protein Sup35 with the sequence GNNQQNY serves as an ideal model for structural understanding of amyloid assembly and kinetics. In this study, we used a reproducible solubilisation protocol that allows the generation of homogenous monomeric solution of GNNQQNY to understand the molecular details of its self-assembly mechanism. The aggregation kinetics data show that the GNNQQNY sequences follow nucleation-dependent aggregation kinetics with a critical nucleus of size ~7 monomers and that the size and efficiency of nucleation was found to be inversely related to the reaction temperature. The generated nucleus reduces the thermodynamic energy barrier by acting as a template for further self-assembly and results in highly ordered amyloid fibrils. The fibers grown at different temperatures showed similar Thioflavin T positivity, Congo red binding and β-sheet rich structures displaying a characteristic cross-β diffraction pattern. These aggregates also share morphological and structural identity with those reported earlier. The mature GNNQQNY fibers exerted no significant oxidative stress or cytotoxicity upon incubating with differentiated SHSY5Y cells. To our knowledge, this is the first study to experimentally validate previous predictions based on theoretical and molecular dynamics simulations. These findings will provide the basis for understanding the kinetics and thermodynamics of amyloid nucleation and elongation of amyloidogenic systems associated with many systemic and neurodegenerative diseases.

Functional Fractionation of Platelets: Aggregation Kinetics and Glycoprotein Labeling of Differing Platelet Populations

1982 ◽  
Vol 48 (02) ◽  
pp. 211-216 ◽  
Author(s):  
V M Haver ◽  
A R L Gear
Keyword(s):  
Galactose Oxidase ◽  
Aggregation Kinetics ◽  
Maximal Rate ◽  
Membrane Glycoproteins ◽  
Whole Cells ◽  
Reversible Aggregation ◽  
Significant Difference ◽  
Small Doses ◽  
Major Loss ◽  
Kinetics Of

SummaryPlatelet heterogeneity has been studied with a technique called functional fractionation which employs gentle centrifugation to yield subpopulations (“reactive” and “less-reactive” platelets) after exposure to small doses of aggregating agent. Aggregation kinetics of the different platelet populations were investigated by quenched-flow aggregometry. The large, “reactive” platelets were more sensitive to ADP (Ka = 1.74 μM) than the smaller “less-reactive” platelets (Ka = 4.08 μM). However, their maximal rate of aggregation (Vmax, % of platelets aggregating per sec) of 23.3 was significantly lower than the “less-reactive” platelets (Vmax = 34.7). The “reactive” platelets had a 2.2 fold higher level of cyclic AMP.Platelet glycoproteins were labeled using the neuraminidase-galactose oxidase – [H3]-NaBH4 technique. When platelets were labeled after reversible aggregation, the “reactive” platelets showed a two-fold decrease in labeling efficiency (versus control platelets). However, examination of whole cells or membrane preparations from reversibly aggregated platelets revealed no significant difference in Coomassie or PAS (Schiff) staining.These results suggest that the large, “reactive” platelets are more sensitive to ADP but are not hyperaggregable in a kinetic sense. Reversible aggregation may cause a re-orientation of membrane glycoproteins that is apparently not characterized by a major loss of glycoprotein material.

In situ Time-Resolved Small-Angle X-ray Scattering Reveals the Formation Kinetics of Polyelectrolyte Complex Micelles

2019 ◽  
Author(s):  
Hao Wu ◽  
Jeffrey Ting ◽  
Siqi Meng ◽  
Matthew Tirrell
Keyword(s):  
Small Angle ◽  
Self Assembly ◽  
Electrostatic Interactions ◽  
Polyelectrolyte Complex ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Kinetics Of ◽  
Ray Scattering

We have directly observed the <i>in situ</i> self-assembly kinetics of polyelectrolyte complex (PEC) micelles by synchrotron time-resolved small-angle X-ray scattering, equipped with a stopped-flow device that provides millisecond temporal resolution. This work has elucidated one general kinetic pathway for the process of PEC micelle formation, which provides useful physical insights for increasing our fundamental understanding of complexation and self-assembly dynamics driven by electrostatic interactions that occur on ultrafast timescales.

Fluorescence biosensor for Salmonella typhimurium detection in food based on nano-self-assembly of alendronic acid modified upconversion and gold nanoparticles

2021 ◽  
Author(s):  
Min Chen ◽  
Leiqing Pan ◽  
K. Tu
Keyword(s):  
Gold Nanoparticles ◽  
Salmonella Typhimurium ◽  
Gold Nanoparticle ◽  
Alendronic Acid ◽  
Self Assembly ◽  
Upconversion Nanoparticles ◽  
Fluorescent Biosensor ◽  
Fluorescence Biosensor

A simple and quick responsive fluorescent biosensor for Salmonella typhimurium detection based on the recognition of aptamer coupled with alendronic acid (ADA)@upconversion nanoparticles (UCNPs) and gold nanoparticle (AuNPs) has been...

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