AlCl(3) solution was analyzed at concentrations from 0.02 to 100 mM using an electrospray ionization quadrupole mass spectrometer (ESI-Q-MS), and the dissolution state of aluminum ions is discussed. Results obtained using ESI-Q-MS were consistent with those obtained using (27)Al nuclear magnetic resonance ((27)Al NMR). Aluminum species existed mainly as positively charged monomeric aluminum hydroxide coordinated with several water molecules in solution. The complexation of chloride ions by aluminum ions differed between the positive and negative ion modes. Chemical reactions that partially modified chemical forms of species through ESI-Q-MS measurement were also observed. In the same aluminum chloride solution, using ESI-TOF-MS and ESI-Q-MS/MS studies, the disagreement of the reports is discussed. It is concluded that ESI-TOF-MS might show also the gas-phase reaction in the mass spectrometer but the dissolution state of aluminum species can be shown by ESI-Q-MS.
The
cross-linked pentapeptides (2R,7R)-diaminooctanedioyl-bis(Tyr-Arg-Leu-Arg-Tyr-amide) ((2R,7R)-BVD-74D, (2R,7R)-1) and octanedioyl-bis(Tyr-Arg-Leu-Arg-Tyr-amide)
(2) as well as the pentapeptide Ac-Tyr-Arg-Leu-Arg-Tyr-amide
(3) were previously described as neuropeptide Y Y4 receptor (Y4R) partial agonists. Here, we report
on a series of analogues of (2R,7R)-1 and 2 in which Arg2, Leu3, or Arg4 were replaced by the respective aza-amino
acids. The replacement of Arg2 in 3 with a
carbamoylated arginine building block and the extension of the N-terminus
by an additional arginine led to the high-affinity hexapeptide Ac-Arg-Tyr-Nω-[(4-aminobutyl)aminocarbonyl]Arg-Leu-Arg-Tyr-amide
(35), which was used as a precursor for a d-amino
acid scan. The target compounds were investigated for Y4R functional activity in assays with complementary readouts: aequorin
Ca2+ and β-arrestin 1 or β-arrestin 2 assays.
In contrast to the parent compounds, which are Y4R agonists,
several ligands were able to suppress the effect elicited by the endogenous
ligand pancreatic polypeptide and therefore represent a novel class
of peptide Y4R antagonists.
The application of electrospray ionization mass spectrometry (ESI-MS) for aluminum speciation in the positive and negative ion modes was discussed. Aluminum nitrate, perchlorate and sulfate solutions were measured by ESI-MS. In the positive ion mode, aluminum species containing anions (Al-L; L=NO3, ClO4 and SO4) were identified, while [Al(OH)2(H2O)n]+ (n=2-4) were the main species. The affinity of the anions with Al3+ estimated by ESI-MS was consistent with the hardness of the anions (hard and soft acids and bases principle) and the results from 27Al nuclear magnetic resonance studies. This indicates that the results observed from the positive ion mode preserved the chemical state of aluminum in the solution. In the negative ion mode, [Al(OH)4-nLn]- (n=0-2, L=NO3, ClO4) were the main species, which were considered to be converted from positive aluminum species, [Al(OH)(H2O)n]+ (n=2-4), by the successive addition of anions. Anions did not only attach to one aluminum ion but also bridged two aluminum ions. In Al2(SO4)3 solution, the behavior of SO4(2-) in the negative ion mode differed from that of NO3- and ClO4-. This may reflect the affinity of SO4(2-) with Al3+ in the solution or in the mass spectrometer or in both. Finally, detection mechanisms for the aluminum species in the solution are proposed for both the positive and negative ion modes. It is shown that ESI-MS can be used to observe the interaction between Al3+ and anions. We show the importance of the interpretation of the results by ESI-MS for obtaining new information of the metal species in the solution.
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