Open AccessBiomimetic Chemistry on Tandem Protein/Lipid Damages under Reductive Radical Stress
Author(s) -
Sı́lvia Atrian,
Krzysztof Bobrowski,
Mercè Capdevila,
Chryssostomos Chatgilialoglu,
Carla Ferreri,
Chantal HouéeLevin,
Anna Maria Salzano,
Andrea Scaloni,
Armida Torreggiani
Publication year - 2008
Publication title -
chimia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.387
H-Index - 55
eISSN - 2673-2424
pISSN - 0009-4293
DOI - 10.2533/chimia.2008.721
Subject(s) - chemistry , native chemical ligation , cysteine , amino acid , biochemistry , radical , combinatorial chemistry , organic chemistry , enzyme
The study of radical stress in the biological environment needs a comprehensive vision of all possible reactive species and their mechanisms. Among them, reductive stress is evaluated for its selective target of sulfur-containing compounds. The selective attack of reducing species like H• atoms or eaq?/H+ to sulfur-containing amino acid residues has been proved in different substrates, peptides and proteins. The transformations include methionine to ?-aminobutyric acid and cysteine/cystine residues to alanine, as recognized in several sequences so far, such as RNase A, lysozyme, Met-enkephalin, amyloid ?-peptide and metallothioneins. The amino acid desulfurization is accompanied by the formation of low-molecular-weight sulfur-centered radicals that may cause geometrical cis–trans isomerization of unsaturated fatty acid residues in lipid bilayer. Thus, tandem protein/lipid damage is accomplished. Progress in research has given us a more comprehensive overview of the protein modifications and their roles, and the chemical biology approach will make its vital contribution to the study of free radical reactions, linking chemistry to biology and medicine.