Stability and dynamics of magnetocapillary interactions.

نویسندگان

  • Rujeko Chinomona
  • Janelle Lajeunesse
  • William H Mitchell
  • Yao Yao
  • Saverio E Spagnolie
چکیده

Recent experiments have shown that floating ferromagnetic beads, under the influence of an oscillating background magnetic field, can move along a liquid-air interface in a sustained periodic locomotion [Lumay et al., Soft Matter, 2013, 9, 2420]. Dynamic activity arises from a periodically induced dipole-dipole repulsion between the beads acting in concert with capillary attraction. We investigate analytically and numerically the stability and dynamics of this magnetocapillary swimming, and explore other related topics including the steady and periodic equilibrium configurations of two and three beads, and bead collisions. The swimming speed and system stability depend on a dimensionless measure of the relative repulsive and attractive forces which we term the magnetocapillary number. An oscillatory magnetic field may stabilize an otherwise unstable collinear configuration, and striking behaviors are observed in fast transitions to and from locomotory states, offering insight into the behavior and self-assembly of interface-bound micro-particles.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Molecular Insight into the Mutual Interactions of Two Transmembrane Domains of Human Glycine Receptor (TM23-GlyR), with the Lipid Bilayers

Appearing as a computational microscope, MD simulation can ‘zoom in’ to atomic resolution to assess detailed interactions of a membrane protein with its surrounding lipids, which play important roles in the stability and function of such proteins. This study has employed the molecular dynamics (MD) simulations, to determine the effect of added DMPC or DMTAP molecules on the structure of D...

متن کامل

Molecular Docking Based on Virtual Screening, Molecular Dynamics and Atoms in Molecules Studies to Identify the Potential Human Epidermal Receptor 2 Intracellular Domain Inhibitors

Human epidermal growth factor receptor 2 (HER2) is a member of the epidermal growth factor receptor family having tyrosine kinase activity. Overexpression of HER2 usually causes malignant transformation of cells and is responsible for the breast cancer. In this work, the virtual screening, molecular docking, quantum mechanics and molecular dynamics methods were employed to study protein–ligand ...

متن کامل

Molecular dynamics simulation and docking studies on the binding properties of several anticancer drugs to human serum albumin

Disposition and transportation of anticancer drugs by human serum albumin (HSA) affects their bioavailability, distribution and elimination. In this study, the interaction of a set of anticancer drugs with HSA was investigated by molecular dynamics and molecular docking simulations. The drugs' activities were analyzed according to their docking scores, binding sites and structural descriptors. ...

متن کامل

Symmetry breaking in a few-body system with magnetocapillary interactions.

We have experimentally investigated the interactions between floating magnetic spheres which are submitted to a vertical magnetic field, ensuring a tunable repulsion, while capillary forces induce attraction. We emphasize the complex arrangements of floating bodies. The equilibrium distance between particles exhibits hysteresis when the applied magnetic field is modified. Irreversible processes...

متن کامل

Molecular Dynamics Simulation and Free Energy Studies on the Interaction of Salicylic Acid with Human Serum Albumin (HSA)

Human serum albumin (HSA) is the most abundant protein in the blood plasma. Molecular dynamics simulations of subdomain IIA of HSA and its complex with salicylic acid (SAL) were performed to investigate structural changes induced by the ligand binding. To estimate the binding affinity of SAL molecule to subdomains IB and IIA in HSA protein, binding free energies were calculated using the Molecu...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Soft matter

دوره 11 9  شماره 

صفحات  -

تاریخ انتشار 2015