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N-homocysteinylation induces different structural and functional consequences on acidic and basic proteins.

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Homocysteine thiolactone (HTL) modifies proteins, causing toxicity linked to cardiovascular and neurodegenerative disorders. Protein isoelectric point (pI) dictates HTL

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Toxicology

Background:

  • Homocysteine toxicity is proposed to involve protein modification by homocysteine thiolactone (HTL).
  • HTL forms covalent adducts with lysine residues, a process termed N-homocysteinylation.
  • N-homocysteinylation is implicated in cardiovascular and neurodegenerative disorders due to protein structural and functional changes.

Purpose of the Study:

  • To investigate the reactivity of HTL with proteins possessing diverse physicochemical properties.
  • To elucidate how protein structure and function are altered by N-homocysteinylation.
  • To determine the influence of protein isoelectric point (pI) on HTL-induced modifications.

Main Methods:

  • Spectroscopic approaches were employed to study protein-HTL interactions.
  • Proteins with varying physicochemical properties were incubated with HTL.
  • Structural and functional alterations in proteins were assessed.

Main Results:

  • N-homocysteinylation exhibited differential effects on acidic and basic proteins.
  • The isoelectric point (pI) of a protein was found to correlate with the extent of N-homocysteinylation.
  • Protein pI influences the degree of structural and functional consequences following homocysteinylation.

Conclusions:

  • The isoelectric point (pI) of a protein is a critical determinant of N-homocysteinylation extent and its pathological outcomes.
  • HTL primarily targets acidic proteins, offering mechanistic insights into HTL-induced neurodegeneration.
  • Understanding pI-dependent homocysteinylation may reveal therapeutic targets for homocysteine toxicity.