The mighty arginine, the stable quaternary amines, the powerful aromatics, and the aggressive phosphate: Their role in the noncovalent minuet

Amina S. Woods

Research output: Contribution to journalArticle

Abstract

In the age of proteomics, the role of certain amino acid residues and some post-translational modifications in noncovalent complex formation are gaining in importance, as the understanding of interactions between biological molecules, is at the heart of the structure function relationship puzzle. In this work, mass spectrometry is used to highlight ammonium- or guanidinium-aromatic interactions through Cation-π bonds and ammonium- or guanidinium-phosphate interactions through salt bridge formation. Such interactions are crucial factors in certain ligand-receptor interactions and receptor-receptor interactions. In addition, the ability of phosphorylated residues and phosphorylated lipids to form noncovalent complexes with guanidinium and quaternary ammonium (mostly through Coulombic interactions) is demonstrated, and could explain the stability of certain membrane embedded protein, or a possible role for phosphorylation in protein-protein interactions. Dougherty's work demonstrates cation-π interactions in intra-protein interactions and folding, the present work explores inter-peptide interactions, i.e., the formation of noncovalent complexes between peptides' epitopes containing adjacent aromatic residues and ones containing adjacent Arg as a model to better understand the role of cation-π complexes in protein-protein interaction. Complexes of peptides containing aromatic residues with quaternary amines as well as the interaction of aromatic compounds, with the guanidinium group of Arg are also investigated. Considering that an inordinate number of therapeutic compounds contain aromatic rings and quaternary amines, the above-described interactions could possibly be of great importance in better understanding their mechanism of action.

Original languageEnglish (US)
Pages (from-to)478-484
Number of pages7
JournalJournal of Proteome Research
Volume3
Issue number3
DOIs
StatePublished - May 2004
Externally publishedYes

Fingerprint

Guanidine
Amines
Arginine
Phosphates
Ammonium Compounds
Cations
Peptides
Aromatic compounds
Proteins
Protein Folding
Post Translational Protein Processing
Phosphorylation
Proteomics
Epitopes
Mass Spectrometry
Membrane Proteins
Salts
Mass spectrometry
Ligands
Lipids

Keywords

  • Noncovalent interactions
  • Phosphate moieties
  • Quaternary amines

ASJC Scopus subject areas

  • Genetics
  • Biotechnology
  • Biochemistry

Cite this

@article{36f41b958e1f4232a68dd1c2c9ccb313,
title = "The mighty arginine, the stable quaternary amines, the powerful aromatics, and the aggressive phosphate: Their role in the noncovalent minuet",
abstract = "In the age of proteomics, the role of certain amino acid residues and some post-translational modifications in noncovalent complex formation are gaining in importance, as the understanding of interactions between biological molecules, is at the heart of the structure function relationship puzzle. In this work, mass spectrometry is used to highlight ammonium- or guanidinium-aromatic interactions through Cation-π bonds and ammonium- or guanidinium-phosphate interactions through salt bridge formation. Such interactions are crucial factors in certain ligand-receptor interactions and receptor-receptor interactions. In addition, the ability of phosphorylated residues and phosphorylated lipids to form noncovalent complexes with guanidinium and quaternary ammonium (mostly through Coulombic interactions) is demonstrated, and could explain the stability of certain membrane embedded protein, or a possible role for phosphorylation in protein-protein interactions. Dougherty's work demonstrates cation-π interactions in intra-protein interactions and folding, the present work explores inter-peptide interactions, i.e., the formation of noncovalent complexes between peptides' epitopes containing adjacent aromatic residues and ones containing adjacent Arg as a model to better understand the role of cation-π complexes in protein-protein interaction. Complexes of peptides containing aromatic residues with quaternary amines as well as the interaction of aromatic compounds, with the guanidinium group of Arg are also investigated. Considering that an inordinate number of therapeutic compounds contain aromatic rings and quaternary amines, the above-described interactions could possibly be of great importance in better understanding their mechanism of action.",
keywords = "Noncovalent interactions, Phosphate moieties, Quaternary amines",
author = "Woods, {Amina S.}",
year = "2004",
month = "5",
doi = "10.1021/pr034091l",
language = "English (US)",
volume = "3",
pages = "478--484",
journal = "Journal of Proteome Research",
issn = "1535-3893",
publisher = "American Chemical Society",
number = "3",

}

TY - JOUR

T1 - The mighty arginine, the stable quaternary amines, the powerful aromatics, and the aggressive phosphate

T2 - Their role in the noncovalent minuet

AU - Woods, Amina S.

PY - 2004/5

Y1 - 2004/5

N2 - In the age of proteomics, the role of certain amino acid residues and some post-translational modifications in noncovalent complex formation are gaining in importance, as the understanding of interactions between biological molecules, is at the heart of the structure function relationship puzzle. In this work, mass spectrometry is used to highlight ammonium- or guanidinium-aromatic interactions through Cation-π bonds and ammonium- or guanidinium-phosphate interactions through salt bridge formation. Such interactions are crucial factors in certain ligand-receptor interactions and receptor-receptor interactions. In addition, the ability of phosphorylated residues and phosphorylated lipids to form noncovalent complexes with guanidinium and quaternary ammonium (mostly through Coulombic interactions) is demonstrated, and could explain the stability of certain membrane embedded protein, or a possible role for phosphorylation in protein-protein interactions. Dougherty's work demonstrates cation-π interactions in intra-protein interactions and folding, the present work explores inter-peptide interactions, i.e., the formation of noncovalent complexes between peptides' epitopes containing adjacent aromatic residues and ones containing adjacent Arg as a model to better understand the role of cation-π complexes in protein-protein interaction. Complexes of peptides containing aromatic residues with quaternary amines as well as the interaction of aromatic compounds, with the guanidinium group of Arg are also investigated. Considering that an inordinate number of therapeutic compounds contain aromatic rings and quaternary amines, the above-described interactions could possibly be of great importance in better understanding their mechanism of action.

AB - In the age of proteomics, the role of certain amino acid residues and some post-translational modifications in noncovalent complex formation are gaining in importance, as the understanding of interactions between biological molecules, is at the heart of the structure function relationship puzzle. In this work, mass spectrometry is used to highlight ammonium- or guanidinium-aromatic interactions through Cation-π bonds and ammonium- or guanidinium-phosphate interactions through salt bridge formation. Such interactions are crucial factors in certain ligand-receptor interactions and receptor-receptor interactions. In addition, the ability of phosphorylated residues and phosphorylated lipids to form noncovalent complexes with guanidinium and quaternary ammonium (mostly through Coulombic interactions) is demonstrated, and could explain the stability of certain membrane embedded protein, or a possible role for phosphorylation in protein-protein interactions. Dougherty's work demonstrates cation-π interactions in intra-protein interactions and folding, the present work explores inter-peptide interactions, i.e., the formation of noncovalent complexes between peptides' epitopes containing adjacent aromatic residues and ones containing adjacent Arg as a model to better understand the role of cation-π complexes in protein-protein interaction. Complexes of peptides containing aromatic residues with quaternary amines as well as the interaction of aromatic compounds, with the guanidinium group of Arg are also investigated. Considering that an inordinate number of therapeutic compounds contain aromatic rings and quaternary amines, the above-described interactions could possibly be of great importance in better understanding their mechanism of action.

KW - Noncovalent interactions

KW - Phosphate moieties

KW - Quaternary amines

UR - http://www.scopus.com/inward/record.url?scp=3042659990&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=3042659990&partnerID=8YFLogxK

U2 - 10.1021/pr034091l

DO - 10.1021/pr034091l

M3 - Article

C2 - 15253429

AN - SCOPUS:3042659990

VL - 3

SP - 478

EP - 484

JO - Journal of Proteome Research

JF - Journal of Proteome Research

SN - 1535-3893

IS - 3

ER -