Complex Formation in Solutions of Oppositely Charged Polyelectrolytes at Different Polyion Compositions and Salt Content†

2003 ◽  
Vol 107 (32) ◽  
pp. 8198-8207 ◽  
Author(s):  
Yoshikatsu Hayashi ◽  
Magnus Ullner ◽  
Per Linse
2016 ◽  
Vol 144 (16) ◽  
pp. 164902 ◽  
Author(s):  
Jiajia Zhou ◽  
Matthias Barz ◽  
Friederike Schmid

Langmuir ◽  
2004 ◽  
Vol 20 (10) ◽  
pp. 3906-3912 ◽  
Author(s):  
Jan Cocquyt ◽  
Ulf Olsson ◽  
Gerd Olofsson ◽  
Paul Van der Meeren

1990 ◽  
Vol 210 ◽  
Author(s):  
Conor J. Twomey ◽  
Shaw H. Chen

AbstractThe complex formation and morphology of the NdCI3—PEO system are presented together with some preliminary results on the Nd(DPM)3 \Nd—tris—2,2,6,6—tetramethyl —3,5—heptane dionate]—PEO system. Although the NdCl3—PEO complex is found to be highly hygroscopic, it is shown that residual moisture can be removed reversibly, thereby permitting the role of water in affecting the morphology of the solid to be examined. It is concluded that complexation is a competitive process between the ether oxygens on the polymer backbone and water. Under anhydrous conditions the resultant complex is amorphous at a \EO]/\NdCl3] molar ratio approximately less than ca. 8, but above this critical value the PEO in excess of the stoichiometric ratio presents a second partially crystalline phase. The glass transition temperatures were found to increase sigmoidally with increasing salt content. Despite the hygroscopic nature of Nd(DPM)3 the resultant complexes were found to be moisture resistant upon prolonged exposure to the atmosphere.


Dendrimers are frequently used for drug molecules delivery to different cells or organs. In our previous papers we used computer simulation to study the complex formation between dendrimers and dendrigrafts with different short regulatory peptides. The goal of present paper is to study interaction and the possibility of complex formation between lysine dendrimer and molecules of therapeutic EDR peptide. The system consisting of one lysine dendrimer of the second generation and 8 or 16 therapeutic EDR peptide molecules in water with explicit counterions was studied by computer simulation. The method of molecular dynamics and full atomic model were used for this goal. It was obtained that EDR peptide molecules become adsorbed by lysine dendrimer and form stable complex with it. Structure and conformational properties of this complex were studied. It was demonstrated that formation of complex occurs mainly due to electrostatic interaction between oppositely charged dendrimer and peptide molecules. Such complexes could be used in future for delivery of these or similar peptide molecules to the targeted tissues and organs.


2005 ◽  
Vol 109 (21) ◽  
pp. 10807-10812 ◽  
Author(s):  
Xiaoyong Wang ◽  
Yajuan Li ◽  
Junxin Li ◽  
Jinben Wang ◽  
Yilin Wang ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document