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. 2019 Apr;25(2):212-218.
doi: 10.1177/1469066718791793.

Histidine, the less interactive cousin of arginine

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Histidine, the less interactive cousin of arginine

Ludovic Muller et al. Eur J Mass Spectrom (Chichester). 2019 Apr.

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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Figures

Figure 1:
Figure 1:
a. MALDI Mass spectrum of a mixture of SHHGLHSTPD (SHH) and SAQEpSQGNT (SAQEpS) showing in: a. NCX peak (m/z 2087). b. MS/MS spectrum of the NCX ion (m/z 2087) with CID 30% of energy.
Figure 2:
Figure 2:
NCX intensity ratio (NCX Intensity/(Intensity(basic peptide)+Intensity(acidic peptide)) for (a) SHHGLHSTPD (SHH), and NLRRITRVN (RRI) and diverse acidic and cyclic peptides, and for (b) SAQEpSQGNT and diverse basic peptides measured by MALDI.
Figure 3:
Figure 3:
ESI Mass spectrum of a. SHH and SAQEpS and b. RRI and SAQEpS. NCX peaks has been enlarged 10 times for SHH.
Figure 4:
Figure 4:
Stability curve of NCX intensity of both basic epitotes (SHH and RRI) with SAQEpSQGNT in function of the HCD collision energy.

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