Tilting and Tumbling of Janus Nanoparticles at Sheared Interfaces.

ACS Nano

Department of Mechanical and Aerospace Engineering, Rutgers, The State University of New Jersey, 98 Brett Road, Piscataway, New Jersey 08854-8058, United States.

Published: May 2016

We investigate the response of a single Janus nanoparticle adsorbed at an oil-water interface to imposed shear flows using molecular dynamics simulations. We consider particles of different geometry, including spheres, cylinders, and discs, and tune their degree of amphiphilicity by controlling the affinity of their two sides to the fluid phases. We observe that depending on the shape, amphiphilicity, and the applied shear rate, two modes of rotational dynamics takes place: a smooth tilt or a tumbling motion. We demonstrate that irrespective of this dynamic behavior, a steady-state orientation is eventually achieved as a result of the balance between the shear- and capillary-induced torques, which can be tuned by controlling the surface property and flow parameters. Our findings provide insight on using flow fields to tune particle orientation at an interface and to utilize it to direct their assembly into ordered monolayers.

Download full-text PDF

Source
http://dx.doi.org/10.1021/acsnano.6b01521DOI Listing

Publication Analysis

Top Keywords

tilting tumbling
4
tumbling janus
4
janus nanoparticles
4
nanoparticles sheared
4
sheared interfaces
4
interfaces investigate
4
investigate response
4
response single
4
single janus
4
janus nanoparticle
4

Similar Publications

Crowding is the interference by surrounding objects (flankers) with target perception. Low target-flanker similarity usually yields weaker crowding than high similarity ('similarity rule') with less interference, e.g.

View Article and Find Full Text PDF

We report on amide (N-H) NMR relaxation from the protein S100A1 analyzed with the slowly relaxing local structure (SRLS) approach. S100A1 comprises two calcium-binding "EF-hands" (helix-loop-helix motifs) connected by a linker. The dynamic structure of this protein, in both calcium-free and calcium-bound form, is described as the restricted local N-H motion coupled to isotropic protein tumbling.

View Article and Find Full Text PDF

Shear-induced polydomain structures of nematic lyotropic chromonic liquid crystal disodium cromoglycate.

Soft Matter

September 2020

Department of Physics, Kent State University, Kent, OH 44242, USA. and Advanced Materials and Liquid Crystal Institute, Kent State University, Kent, OH 44242, USA and Materials Science Graduate Program, Kent State University, Kent, OH 44242, USA.

Lyotropic chromonic liquid crystals (LCLCs) represent aqueous dispersions of organic disk-like molecules that form cylindrical aggregates. Despite the growing interest in these materials, their flow behavior is poorly understood. Here, we explore the effect of shear on dynamic structures of the nematic LCLC, formed by 14 wt% water dispersion of disodium cromoglycate (DSCG).

View Article and Find Full Text PDF

The relation between co- and post-translational protein folding and aggregation in the cell is poorly understood. Here, we employ a combination of fluorescence anisotropy decays in the frequency domain, fluorescence-detected solubility assays, and NMR spectroscopy to explore the role of the ribosome in protein folding within a biologically relevant context. First, we find that a primary function of the ribosome is to promote cotranslational nascent-protein solubility, thus supporting cotranslational folding even in the absence of molecular chaperones.

View Article and Find Full Text PDF

Diatoms are one of the earth's major oxygen producers. For that reason, studying the floating phenomena of living diatom cells in water is an important research subject. Efficiency of photosynthesis of diatom cells may be heavily affected by their floating behavior.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!