scholarly journals Peripheral myelin of Xenopus laevis: Role of electrostatic and hydrophobic interactions in membrane compaction

2008 ◽  
Vol 162 (1) ◽  
pp. 170-183 ◽  
Author(s):  
XiaoYang Luo ◽  
Jana Cerullo ◽  
Tamara Dawli ◽  
Christina Priest ◽  
Zaid Haddadin ◽  
...  
1981 ◽  
Vol 59 (13) ◽  
pp. 1978-1986 ◽  
Author(s):  
R. Bennes ◽  
B. E. Conway

By means of adsorption and surface-potential studies on a series of R4−nN+Hn perchlorates at the air/water interface, the role of hydrophobic and hydrophilic interaction in the adsorption and ion distribution of these salts near the air/water interface is examined. While the adsorption of the alkylamine ions increases as n decreases from three to zero, inclusive, the surface-potential change accompanying the adsorption decreases. This effect is interpreted in terms of opposing hydrophilic, electrostatic and hydrophobic interactions between the organic ion and water near the liquid surface, leading to a progressive change of double-layer ion distribution. In Part II, comparative studies of the same series of compounds at the Hg/water interface are reported.


The red cell sialoglycoproteins (glycophorins, The red cell sialoglycoproteins (glycophorins, α(A), δ(B) and β and γ(C)) play a crucial role in the invasion of human red cells by merozoites of Plasmodium falciparum . Red cells deficient in any of the glycophorins, including β (also known as glycoconnectin), resist infection by this parasite to varying degrees. These cells and other naturally occurring well-characterized glycophorin variants provide extremely powerful tools to dissect the role of these molecules in invasion. The binding of merozoites to human red cells appears analogous to the binding of wheatgerm agglutinin to sialoglycoconjugates. In both systems O- and N-linked oligosaccharides may be involved. Membrane lipid has not been implicated as a receptor for merozoites, but may instead non-specifically modify binding, as may electrostatic and hydrophobic interactions. The results of data using monoclonal antibodies and lectins, although possibly helpful in identifying specific determinants, must be interpreted with caution. Overall the data suggest that the red cell receptors for all strains of P. falciparum tested to date are located on the glycophorins. Accordingly these putative receptors have been used to affinity-purify complementary parasite components which may yet prove to be of protective immunological significance in a vaccine.


2015 ◽  
Vol 104 (2) ◽  
pp. 577-586 ◽  
Author(s):  
Reza Esfandiary ◽  
Arun Parupudi ◽  
Jose Casas-Finet ◽  
Dhanesh Gadre ◽  
Hasige Sathish

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Misbah Iram ◽  
Hamadia Sultana ◽  
Muhammad Usman ◽  
Bazgha Ahmad ◽  
Nadia Akram ◽  
...  

Abstract Interaction of sulphone based reactive dyes, designated as dye-1 and dye-2, with cationic micellar system of cetyltrimethylammonium bromide (CTAB), has been investigated by spectroscopic and conductometeric measurements. Efficiency of the selected micellar systems is assessed by the values of binding constant (K b ), partition coefficient (K x ) and respective Gibbs energies. Critical micelle concentration (CMC) of surfactant, electrostatic and hydrophobic interactions as well as polarity of the medium plays significant role in this phenomenon. The negative values of Gibbs energies of binding (∆G b ) and partition (∆G p ) predicts the feasibility and spontaneity of respective processes. Similarly negative values of ∆G m and ∆H m and positive values of ∆S m , calculated from conductometeric data, further, revealed the exothermicity, spontaneity and, thus, stability of system. The results, herein, have disclosed the strong interaction between dye and surfactant molecules. The dye-2 has been observed to be solubilized to greater extent, as compared to dye 1, due to strong interaction ith hydrophiles of CTAB and accommodation of its molecules in palisade layer of micelle closer to the micelle/water interface.


1998 ◽  
Vol 37 (10-11) ◽  
pp. 1381-1391 ◽  
Author(s):  
Changhai Cu ◽  
Robert Bähring ◽  
Mark L. Mayer

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