Complex Formation of Nickel(II) with Sugar Residues, Nucleobases, Phosphates, Nucleotides, and Nucleic Acids

Author(s):  
Roland K. O. Sigel ◽  
Helmut Sigel
2012 ◽  
Vol 41 (1) ◽  
pp. 327-339 ◽  
Author(s):  
Paola Cavaliere ◽  
Bruno Pagano ◽  
Vincenzo Granata ◽  
Stephanie Prigent ◽  
Human Rezaei ◽  
...  

2006 ◽  
Vol 6 (11) ◽  
pp. 3532-3538
Author(s):  
Khee Dong Eom ◽  
Jin Sook Kim ◽  
Sun Mi Park ◽  
Myong Soo Kim ◽  
Rina Yu ◽  
...  

A series of nano-sized dendritic α,ε-poly(L-lysine)s (DPL) were synthesized by the solid-phase peptide synthesis method, using a core ε-peptide structure consisting of eight lysine residues. Surface amines of dendritic α,ε-poly(L-lysine) were characterized by comparing the retention times of a reverse phase HPLC with the electrophoretic mobilities of capillary zone electrophoresis (CZE) and non-denatured polyacrylamide gel electrophoresis (PAGE). The elution times of α,ε-poly(L-lysine) in HPLC were well correlated with the electrophoretic mobilities of CZE and PAGE. The separation was dependent on size, shape of molecule and the number of surface amine. The α,ε-poly(L-lysine) formed a complex with nucleic acids at various charge ratios and the degree of complex formation was size- and structure-dependent. Atomic force microscopy of the complex visualized the size and morphology of α,ε-poly(L-lysine)/DNA complex as a nano-sized spherical shape. The small size in complex formation provides a promise for in vivo therapeutic application of dendritic α,ε-poly(L-lysine)s or their derivatives in the delivery of gene or oligonucleotide.


BIOPHYSICS ◽  
2014 ◽  
Vol 59 (4) ◽  
pp. 546-551 ◽  
Author(s):  
V. V. Kostjukov ◽  
O. V. Rogova ◽  
M. P. Evstigneev

2013 ◽  
Vol 91 (6) ◽  
pp. 759-770 ◽  
Author(s):  
Victoria Tüngler ◽  
Wolfgang Staroske ◽  
Barbara Kind ◽  
Manuela Dobrick ◽  
Stefanie Kretschmer ◽  
...  

Blood ◽  
2013 ◽  
Vol 122 (2) ◽  
pp. 272-281 ◽  
Author(s):  
Miriam E. Jaax ◽  
Krystin Krauel ◽  
Thomas Marschall ◽  
Sven Brandt ◽  
Julia Gansler ◽  
...  

Key PointsPF4 binds to nucleic acids and thereby exposes the epitope to which anti-PF4/heparin antibodies bind. PF4/aptamer complexes can induce an immune response resembling heparin-induced thrombocytopenia.


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