Nucleotide recognition in water by a guanidinium-based artificial tweezer receptor

The water-soluble tweezer receptor 1 with two symmetric peptidic arms, which are connected by an aromatic scaffold and contain lysine, phenylalanine, and a guanidinium-based anion-binding site as headgroup, has been synthesized. UV/Vis-derived Job plots show that the receptor forms 1:1 complexes with nucleotides and phosphate in buffered water at neutral pH. Binding constants have been determined by fluorescence and UV/Vis spectroscopy. All nucleotides tested were bound very efficiently, even in pure water, with binding constants between 10(4) and 10(5) M(-1) . Interestingly, all mononucleotides were bound much stronger than phosphate by a factor of at least 5 to 10. Furthermore 1 favors the binding of adenosine monophosphate (AMP) over adenosine diphosphate (ADP) and adenosine triphosphate (ATP), which is unprecedented for artificial nucleotide receptors reported so far. According to NMR spectroscopy and molecular modeling studies, the efficient binding is a result of strong electrostatic contacts supported by π-π interactions with the nucleobase within the cavity-shaped receptor.     

IONS CONFINEMENT IN ELECTRON BEAM ION TRAP

This paper shows the evolution of density and temperature of multi-charged ions in an electron beam ion trap (EBIT). Three cases are studied: the continuous neutral gas injection, ion source injection, and evaporative cooling. The effects of the neutral gas density, axial potential, and the beam current density on the ions evolution are discussed.     

Plasmonically active micron-sized beads for integrated solid-phase synthesis and label-free SERS analysis

Self-assembly of gold nanospheres with a very thin glass shell onto the surface of beads yields a plasmonically active micron-sized substrate for integrated solid-phase synthesis and label-free SERS analysis. The proof-of-principle of this approach is demonstrated by the vibrational spectroscopic discrimination of three distinct amino acids and a dipeptide.