Mechanics of adhesive contact on a power-law graded elastic half-space

We consider adhesive contact between a rigid sphere of radius R and a graded elastic half-space with Young's modulus varying with depth according to a power law E = E-0(z/c(0))(k) (0 < k < 1) while Poisson's ratio v remaining a constant. Closed-form analytical solutions are established for the critical force, the critical radius of contact area and the critical interfacial stress at pull-off. We highlight that the pull-off force has a simple solution of P-cr= -(k+3)pi R Delta gamma/2 where Delta gamma is the work of adhesion and make further discussions with respect to three interesting limits: the classical JKR solution when k = 0, the Gibson solid when k --> 1 and v = 0.5, and the strength limit in which the interfacial stress reaches the theoretical strength of adhesion at pull-off. (C) 2009 Elsevier Ltd. All rights reserved.

Adhesive behavior of two-dimensional power-law graded materials

In this paper, we investigate the adhesive contact between a rigid cylinder of radius R and a graded elastic half-space with a Young's modulus varying with depth according to a power-law, E = E-0(y/c(0))(k) (0 < k < 1), while the Poisson's ratio v remains constant. The results show that, for a given value of ratio R/C-0, a critical value of k exists at which the pull-off force attains a maximum; for a fixed value of k, the larger the ratio R/c(0), the larger the pull-off force is. For Gibson materials (i.e., k = 1 and v = 0.5), closed-form analytical solutions can be obtained for the critical contact half-width at pull-off and pull-off force. We further discuss the perfect stick case with both externally normal and tangential loads.

Insights into the mechanism of human erythrocyte hexose transport : a transferred NOE study of glucose binding to GLUT1

This study examines binding of α- and β-D-glucose in their equilibrium mixture to the glucose transporter (GLUT1) in human erythrocyte membrane preparations by an ^1H NMR method, the transferred NOE (TRNOE). This method is shown theoretically and experimentally to be a sensitive probe of weak ligand-macromolecule interactions. The TRNOEs observed are shown to arise solely from glucose binding to GLUT1. Sites at both membrane faces contribute to the TRNOEs. Binding curves obtained are consistent with a homogeneous class of sugar sites, with an apparent K_D which varies (from ~30 mM to ~70 mM for both anomers) depending on the membrane preparation examined. Preparations with a higher proportion of the cytoplasmic membrane face exposed to bulk solution yield higher apparent KK_Ds. The glucose transport inhibitor cytochalasin B essentially eliminates the TRNOE. Nonlinearity was found in the dependence on sugar concentration of the apparent inhibition constant for cytochalasin B reversal of the TRNOE observed in the α anomer (and probably the β anomer); such nonlinearity implies the existence of ternary complexes of sugar, inhibitor and transporter. The inhibition results furthermore imply the presence of a class of relatively high-affinity (K_D < 2mM) sugar sites specific for the α anomer which do not contribute to NMR-observable binding. The presence of two classes of sugar-sensitive cytochalasin B sites is also indicated. These results are compared with predictions of the alternating conformer model of glucose transport. Variation of apparent K_D in the NMR-observable sites, the formation of ternary complexes and the presence of an anomer-specific site are shown to be inconsistent with this model. An alternate model is developed which reconciles these results with the known transport behavior of GLUT1. In this model, the transporter possesses (at minimum) three classes of sugar sites: (i) transport sites, which are alternately exposed to the cytoplasmic or the extracellular compartment, but never to both simultaneously, (ii) a class of sites (probably relatively low-affinity) which are confined to one compartment, and (iii) the high-affinity α anomer-specific sites, which are confined to the cytoplasmic compartment.