1. Structure of Supramers Formed by the Amphiphile Biotin-CMG-DOPE
- Author
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Alexander B. Tuzikov, Eleonora V. Shtykova, Roman G. Efremov, Daria O. Solovyeva, Stephen Henry, Pavel E. Volynsky, Marcel Schaefer, Vladimir Oleinikov, Nicolai V. Bovin, Ivan Vaskan, Elena Korchagina, Ivan M. Ryzhov, Anton Zalygin, Konstantin Mochalov, and Alexey V. Nizovtsev
- Subjects
Streptavidin ,Protein Conformation ,Surface Properties ,Supramolecular chemistry ,Biotin ,supramers ,Molecular Dynamics Simulation ,010402 general chemistry ,01 natural sciences ,Micelle ,Cover Profile ,lcsh:Chemistry ,Molecular dynamics ,chemistry.chemical_compound ,Amphiphile ,Molecule ,function-spacer-lipid ,amphiphiles ,Full Paper ,010405 organic chemistry ,Phosphatidylethanolamines ,Cover Pictures ,technology, industry, and agriculture ,molecular dynamics simulations ,General Chemistry ,Full Papers ,molecular dynamics ,0104 chemical sciences ,Crystallography ,lcsh:QD1-999 ,chemistry ,ddc:540 ,lipids (amino acids, peptides, and proteins) ,Hydrophobic and Hydrophilic Interactions ,Layer (electronics) - Abstract
ChemistryOpen 9(6), 641 - 648 (2020). doi:10.1002/open.201900276, The synthetic function‐spacer‐lipid (FSL) amphiphile biotin‐CMG‐DOPE is widely used for delicate ligation of living cells with biotin residues under physiological conditions. Since this molecule has an “apolar‐polar‐hydrophobic” gemini structure, the supramolecular organization is expected to differ significantly from the classical micelle. Its organization is investigated with experimental methods and molecular dynamics simulations (MDS). Although the linear length of a single biotin‐CMG‐DOPE molecule is 9.5 nm, the size of the dominant supramer globule is only 14.6 nm. Investigations found that while the DOPE tails form a hydrophobic core, the polar CMG spacer folds back upon itself and predominantly places the biotin reside inside the globule or planar layer. MDS demonstrates that, Published by Wiley-VCH-Verl., Weinheim
- Published
- 2020