We are proposing a new technique for studying interaction of charged biomolecules. It is based on a difference between nitrate and chloride anion influence on electrostatic interactions in order to detect the role of positively charged guanidine groups of proteins. This comparison was demonstrated for human serum albumin (HSA) interaction with a fluorescent reporter, CAPIDAN. Nitrate anions lower their binding constant (K). There are two causes that are responsible for that K decrease induced by nitrate. The first, rise of the ionic strength (like to chloride), and the second, a specific one: at the same concentration and ionic strength nitrate anion more significantly lowers K than chloride anion. The study of electric conductivity of chloride and nitrate salts shows that nitrate anions better than chloride anions form complexes with gu-anidine cations. Therefore it can be assumed that the nitrate-chloride techniques detect a direct contact of negatively charged carboxyl of CAPIDAN with positively charged arginine residues of HSA. HSA site I includes Arg 218 and Arg 222. It is possible that the CAPIDAN carboxyl binds to one of these arginines.
| Published in | European Journal of Biophysics (Volume 1, Issue 2) |
| DOI | 10.11648/j.ejb.20130102.12 |
| Page(s) | 22-27 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
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Copyright © The Author(s), 2024. Published by Science Publishing Group |
Human Serum Albumin, Drug-Binding Site, Ngatively Charged Ligands, Nitrate Anion Blocking Arginine Charge, Fluorescent Probe CAPIDAN
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APA Style
Smolina N. V., Dobretsov G. E., Syrejshchikova T. I., Gamburg Yu. D., Kalinina V. V., et al. (2013). Nitrate Anion as a Probe for Electrostatic Interactions in Complexes Protein-Ligand. European Journal of Biophysics, 1(2), 22-27. https://doi.org/10.11648/j.ejb.20130102.12
ACS Style
Smolina N. V.; Dobretsov G. E.; Syrejshchikova T. I.; Gamburg Yu. D.; Kalinina V. V., et al. Nitrate Anion as a Probe for Electrostatic Interactions in Complexes Protein-Ligand. Eur. J. Biophys. 2013, 1(2), 22-27. doi: 10.11648/j.ejb.20130102.12
AMA Style
Smolina N. V., Dobretsov G. E., Syrejshchikova T. I., Gamburg Yu. D., Kalinina V. V., et al. Nitrate Anion as a Probe for Electrostatic Interactions in Complexes Protein-Ligand. Eur J Biophys. 2013;1(2):22-27. doi: 10.11648/j.ejb.20130102.12
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Download@article{10.11648/j.ejb.20130102.12,
author = {Smolina N. V. and Dobretsov G. E. and Syrejshchikova T. I. and Gamburg Yu. D. and Kalinina V. V. and Gryzunov Yu. A.},
title = {Nitrate Anion as a Probe for Electrostatic Interactions in Complexes Protein-Ligand},
journal = {European Journal of Biophysics},
volume = {1},
number = {2},
pages = {22-27},
doi = {10.11648/j.ejb.20130102.12},
url = {https://doi.org/10.11648/j.ejb.20130102.12},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ejb.20130102.12},
abstract = {We are proposing a new technique for studying interaction of charged biomolecules. It is based on a difference between nitrate and chloride anion influence on electrostatic interactions in order to detect the role of positively charged guanidine groups of proteins. This comparison was demonstrated for human serum albumin (HSA) interaction with a fluorescent reporter, CAPIDAN. Nitrate anions lower their binding constant (K). There are two causes that are responsible for that K decrease induced by nitrate. The first, rise of the ionic strength (like to chloride), and the second, a specific one: at the same concentration and ionic strength nitrate anion more significantly lowers K than chloride anion. The study of electric conductivity of chloride and nitrate salts shows that nitrate anions better than chloride anions form complexes with gu-anidine cations. Therefore it can be assumed that the nitrate-chloride techniques detect a direct contact of negatively charged carboxyl of CAPIDAN with positively charged arginine residues of HSA. HSA site I includes Arg 218 and Arg 222. It is possible that the CAPIDAN carboxyl binds to one of these arginines.},
year = {2013}
}
TY - JOUR T1 - Nitrate Anion as a Probe for Electrostatic Interactions in Complexes Protein-Ligand AU - Smolina N. V. AU - Dobretsov G. E. AU - Syrejshchikova T. I. AU - Gamburg Yu. D. AU - Kalinina V. V. AU - Gryzunov Yu. A. Y1 - 2013/06/10 PY - 2013 N1 - https://doi.org/10.11648/j.ejb.20130102.12 DO - 10.11648/j.ejb.20130102.12 T2 - European Journal of Biophysics JF - European Journal of Biophysics JO - European Journal of Biophysics SP - 22 EP - 27 PB - Science Publishing Group SN - 2329-1737 UR - https://doi.org/10.11648/j.ejb.20130102.12 AB - We are proposing a new technique for studying interaction of charged biomolecules. It is based on a difference between nitrate and chloride anion influence on electrostatic interactions in order to detect the role of positively charged guanidine groups of proteins. This comparison was demonstrated for human serum albumin (HSA) interaction with a fluorescent reporter, CAPIDAN. Nitrate anions lower their binding constant (K). There are two causes that are responsible for that K decrease induced by nitrate. The first, rise of the ionic strength (like to chloride), and the second, a specific one: at the same concentration and ionic strength nitrate anion more significantly lowers K than chloride anion. The study of electric conductivity of chloride and nitrate salts shows that nitrate anions better than chloride anions form complexes with gu-anidine cations. Therefore it can be assumed that the nitrate-chloride techniques detect a direct contact of negatively charged carboxyl of CAPIDAN with positively charged arginine residues of HSA. HSA site I includes Arg 218 and Arg 222. It is possible that the CAPIDAN carboxyl binds to one of these arginines. VL - 1 IS - 2 ER -
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