Premium
Influence of magnetic fields on the hydration process of amino acids: Vibrational spectroscopy study of L‐phenylalanine and L‐glutamine
Author(s) -
De Ninno Antonella,
Castellano Agostina Congiu
Publication year - 2014
Publication title -
bioelectromagnetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.435
H-Index - 81
eISSN - 1521-186X
pISSN - 0197-8462
DOI - 10.1002/bem.21823
Subject(s) - chemistry , protonation , glutamine , molecule , amino acid , aqueous solution , fourier transform infrared spectroscopy , phenylalanine , hydrogen bond , spectroscopy , dissociation (chemistry) , attenuated total reflection , deprotonation , glutamic acid , infrared spectroscopy , analytical chemistry (journal) , organic chemistry , ion , biochemistry , physics , quantum mechanics
Attenuated total reflectance Fourier transform infrared (ATR‐FTIR) spectroscopy has been used to investigate the effect of weak electromagnetic fields on the structure of L ‐glutamine ( L ‐Gln) and L ‐phenylalnine ( L ‐Phe) in aqueous solution. It has been found that the exposure to a DC field or a 50 Hz AC field, for a short time induces modifications in the spectra of exposed samples in agreement with our preceding observations on glutamic acid. Furthermore, the acid–base equilibrium has been investigated by using the ratio of the intensity of the deprotonated on protonated species. In the case of L ‐Phe, the exposure induces a measurable shift of acid dissociation constant pK a 1 out of the experimental errors, while in case of L ‐Gln, the effect is under the limit detectable with this method. The phenomenon of the shift of the acid–base equilibrium has been connected elsewhere to modification of the water–water hydrogen bonds in the water around both the backbone and the residue (R). Here we suggest that the magnetic field modifies the water structure around the molecules and changes the hydrophobic interactions allowing the molecules of amino acids to aggregate. The differences observed in the behavior of L ‐Phe and L ‐Gln may be related to the differences in the polarity of their residues. Bioelectromagnetics. 35:129–135, 2014. © 2013 Wiley Periodicals, Inc.