Self-aggregation and microhydration mechanisms of monoethanolamine: Far-infrared identification of large-amplitude hydrogen bond libration.

The strong tendency for self-aggregation together with an intriguing mechanism for the microhydration of monoethanolamine (MEA) have been explored by low-temperature far-infrared cluster spectroscopy in doped neon "quantum" matrices at 4 K complemented by high-level quantum chemical modeling. In addition to the assignment of new mid-infrared perturbed intramolecular transitions, a distinct far-infrared transition is unambiguously assigned to the concerted large-amplitude hydrogen bond librational motion of the MEA homodimer. This observation confirms a global "head-to-head" intermolecular potential energy minimum associated with the formation of a compact doubly intermolecular OH⋯N hydrogen-bonded cyclic structure, where both monomeric intramolecular OH⋯N hydrogen bonds are broken upon complexation.

Using surfactants as matrix for the matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF-MS) of amino acids: Sodium dodecyl sulfate (SDS) and sodium octyl sulfate (SOS).

In the present study, the applicability of two surfactants including sodium dodecyl sulfate (SDS) and sodium octyl sulfate (SOS) as the matrix for the Matrix-Assisted Laser Desorption/Ionization (MALDI) of several amino acids (phenylalanine (Phe), valine (Val), proline (Pro), alanine (Ala), and tyrosine (Tyr)) is investigated. Also, the effect of the material of the repeller plate of the ionization part of the used time of flight (TOF) mass spectrometer on the spectral patterns of the amino acids is studied. Furthermore, the recorded MALDI spectra of amino acids are compared with their corresponding direct laser desorption/ionization (direct-LDI) TOF mass spectra.