Comparison of stress patterns and displacement in conventional cantilever fixed partial denture with resin bonded cantilever fixed partial denture: A finite element analysis.

Aim: This study aims to analyze the stress patterns and displacement in the cantilever resin bonded fixed partial denture (RBFPD) and compare it with the conventional cantilever fixed partial denture using 3-D finite element analysis. Also, the effect of cement on the displacement and stress patterns in conventional cantilever fixed partial denture was to be analyzed. Materials and Methods: Three-dimensional models were prepared layer wise to depict the conventional cantilever and the cantilever RBFPD. Once the models were made, the material properties were assigned and divided into three groups. (2-conventional cantilever with resin cement, 1- conventional cantilever with GIC cement and 3-resin bonded cantilever with resin cement). Load was applied in vertical as well as lateral directions and the stress patterns along with displacement were analyzed. Results: The results revealed that the von Mises stresses in all the three groups were found to be almost equal under vertical loading. Under lateral loading, the stress was more in cantilever RBFPD. Displacement in all the three axes was significantly less in the cantilever RBFPD. Conclusion: Stress concentration in the lateral direction in cantilever RBFPD was found to be higher than the cantilever conventional group. Displacement in X, Y and Z axes was less in cantilever RBFPD.

Identification of amino groups in the carbohydrate binding activity of winged bean acidic agglutinin.

Chemical modification studies reveal that the modification of amino groups in WBA II leads to a complete loss in the hemagglutinating and saccharide binding activities. Since WBA II is a dimeric molecule and contains two binding sites, one amino group in each of the binding sites is inferred to be essential for its activity. The presence of amino group which has a potential to form hydrogen bonded interactions with the ligand, substantiates our observation regarding the forces involved in WBA II-receptor and WBA II-simple sugar interactions.

Mechanism of lectin-cell interactions: thermodynamic and kinetic analysis of the binding of winged bean acidic lectin (WBA II) to human erythrocytes.

In order to identify the forces involved in the binding and to understand the mechanism involved, equilibrium and kinetic studies were performed on the binding of the winged bean acidic lectin to human erythrocytes. The magnitudes of delta S and delta H were positive and negative respectively, an observation differing markedly from the lectin-simple sugar interactions where delta S and delta H are generally negative. Analysis of the sign and magnitudes of these values indicate that ionic and hydrogen bonded interactions prevail over hydrophobic interactions resulting in net -ve delta H (-37.12 kJ.mol-1) and +ve delta S (14.4 J.mole-1 K-1 at 20 degrees C), thereby suggesting that this entropy driven reaction also reflects conformational changes in the lectin and/or the receptor. Presence of two kinds of receptors for WBA II on erythrocytes, as observed by equilibrium studies, is consistent with the biexponential dissociation rate constants (at 20 degrees C K1 = 1.67 x 10(-3) M-1 sec-1 and K2 = 11.1 x 10(-3) M-1 sec-1). These two rate constants differed by an order of magnitude accounting for the difference in the association constants of the two receptors of WBA II. However, the association process remains monoexponential suggesting no observable difference in the association rates of the lectin molecule with both the receptors, under the experimental conditions studied. The thermodynamic parameters calculated from kinetic data correlate well with those observed by equilibrium. A two-step binding mechanism is proposed based on the kinetic parameters for WBA II-receptor interaction.(ABSTRACT TRUNCATED AT 250 WORDS)