Histidine, the less interactive cousin of arginine
- PMID: 31018697
- PMCID: PMC8269955
- DOI: 10.1177/1469066718791793
Histidine, the less interactive cousin of arginine
Abstract
Electrostatic interactions are one of the main factors influencing biomolecular conformation. The formation of noncovalent complexes by electrostatic interactions is governed by certain amino acid residues and post-translational modifications. It has been demonstrated that adjacent arginine forms noncovalent complex with phosphate; however, histidine noncovalent complexes have rarely been investigated. In the present work, we compare the interaction between basic epitopes (NLRRITRVN, SHHGLHSTPD) and diverse acidic and aromatic-rich peptides using both MALDI and ESI Mass spectrometry. We show that adjacent histidines can also form stable noncovalent bonds and that those bonds are probably formed by a salt bridge between the phosphate or the acid residues and the histidines. However, noncovalent complexes with the arginine epitopes form more readily and are stronger than those with histidine-containing epitopes.
Keywords: Arginine; histidine; mass spectrometry; noncovalent complexes; noncovalent interactions; phosphate.
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References
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- Schug KA and Lindner W. Noncovalent binding between guanidium and anionic groups: focus on biological- and synthetic-based arginine/guanidinium interactions with phosph[on]ate and sulf[on]ate residues. Chem. Rev 2005; 105: 67–114. - PubMed
-
- Woods AS, Ciruela F, Fuxe K, et al. Role of electrostatic interaction in receptor-receptor heteromerization. J. Mol. Neurosci 2005; 26: 125–132. - PubMed
-
- Kovacic P, Draskovich CD and Pozos RS. Unifying electrostatic mechanism for phosphates and sulfates in cell signaling. J. Recept. Signal. Transduct 2007; 27: 433–443. - PubMed
-
- Langner M and Kubica K. The electrostatics of lipid surfaces. Chem. Phys. Lipids 1999; 101: 3–35. - PubMed
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