Mussels use a variety of 3, 4-dihydroxyphenyl-l-alanine (DOPA) rich proteins specifically tailored to adhering to wet surfaces. Synthetic polypeptide analogues of adhesive mussel foot proteins (specifically mfp-3) are used to study the role of DOPA in adhesion. The mussel-inspired peptide is a random copolymer of DOPA and N(5) -(2-hydroxyethyl)-l-glutamine synthesized with DOPA concentrations of 0-27 mol% and molecular weights of 5.
View Article and Find Full Text PDFWe consider the adhesive interaction energy between a pair of vesicles in the strong adhesion limit, in which bending forces play a negligible role in determining vesicle shape compared to forces due to membrane stretching. Although force−distance or energy−distance relationships characterizing adhesive interactions between fluid bilayers are routinely measured using the surface forces apparatus, the atomic force microscope, and the biomembrane force probe, the interacting bilayers in these methods are supported on surfaces (e.g.
View Article and Find Full Text PDFAfter nearly 30 years of research on the hydrophobic interaction, the search for the hydrophobic force law is still continuing. Indeed, there are more questions than answers, and the experimental data are often quite different for nominally similar conditions, as well as, apparently, for nano-, micro-, and macroscopic surfaces. This has led to the conclusion that the experimentally observed force-distance relationships are either a combination of different 'fundamental' interactions, or that the hydrophobic force-law, if there is one, is complex--depending on numerous parameters.
View Article and Find Full Text PDFThe interactions of supported cationic surfactant bilayers and the effects of nonadsorbing cationic polyelectrolytes on these interactions were studied using the surface forces apparatus (SFA) technique. Bilayers of the cationic surfactant di(tallow ethyl ester) dimethyl ammonium chloride (DEEDMAC) were deposited on mica surfaces using the Langmuir-Blodgett technique, and the interactions between the bilayers were measured in various salt, nonionic polymer (PEG), and cationic polyelectrolyte solutions at different polymer molecular weights and concentrations. The forces between the bilayers in CaCl(2) solution are purely repulsive and follow the DLVO theory quantitatively down to bilayer separations of ∼2 nm.
View Article and Find Full Text PDFWe have investigated the formation of phospholipid bilayers of the neutral (zwitterionic) lipid dimyristoyl-phosphatidylcholine (DMPC) on various glass surfaces from vesicles in various aqueous solutions and temperatures using a number of complementary techniques: the surface forces apparatus (SFA), quartz crystal microbalance (QCM), fluorescence recovery after photobleaching (FRAP), fluorescence microscopy, and streaming potential (SP) measurements. The process involves five stages: vesicle adhesion to the substrate surfaces via electrostatic and van der Waals forces, steric interactions with neighboring vesicles, rupture, spreading via hydrophobic fusion of bilayer edges, and ejection of excess lipid, trapped water, and ions into the solution. The forces between DMPC bilayers and silica were measured in the SFA in phosphate buffered saline (PBS), and the adhesion energy was found to be 0.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2009
Actin protein is a major component of the cell cytoskeleton, and its ability to respond to external forces and generate propulsive forces through the polymerization of filaments is central to many cellular processes. The mechanisms governing actin's abilities are still not fully understood because of the difficulty in observing these processes at a molecular level. Here, we describe a technique for studying actin-surface interactions by using a surface forces apparatus that is able to directly visualize and quantify the collective forces generated when layers of noninterconnected, end-tethered actin filaments are confined between 2 (mica) surfaces.
View Article and Find Full Text PDFWe describe two ways to measure normal and/or lateral forces between two surfaces in a surface forces apparatus (SFA) while an electric field is applied between the surfaces. The first method involves depositing thin conductive layers on the exposed substrate (usually mica) sheets; the second involves using the optically reflecting silver layers on the back surfaces of the sheets as the electrodes. Two types of experiments were performed using these new techniques: (1) measuring the effects of an electric field on the rheology of an approximately 40-microm-thick film of zeolite particles suspended in silicone oil and (2) a dynamic study of electric field-induced pattern formation of a thin polymer film.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
March 2007
Mussels adhere to a variety of surfaces by depositing a highly specific ensemble of 3,4-dihydroxyphenyl-l-alanine (DOPA) containing proteins. The adhesive properties of Mytilus edulis foot proteins mfp-1 and mfp-3 were directly measured at the nano-scale by using a surface forces apparatus (SFA). An adhesion energy of order W approximately 3 x 10(-4) J/m(2) was achieved when separating two smooth and chemically inert surfaces of mica (a common alumino-silicate clay mineral) bridged or "glued" by mfp-3.
View Article and Find Full Text PDFPhys Rev E Stat Nonlin Soft Matter Phys
January 2007
Jamming and force networks observed in electrorheological (ER) fluids bear many similarities to those observed in various granular and colloidal systems. We have measured the time evolution (transient stresses) of filamentous networks of colloidal particles in suspensions subjected to continuous tensile strain concomitant with the switching on and off of electric fields. The density of particle chains was found to increase exponentially with the applied tensile strain via a rapid formation of single chains followed by a slower coarsening (aggregation) of the chains.
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