Conformational changes in DNAand protein biomolecules in the pathogenesis of ischemic stroke

The study assessed conformational changes in DNA and protein biomolecules during ischemic stroke (IS) of varying severity using RAMAN spectroscopy. In patients with IS, the conformational structure of hemoporphyrin changes and, as a consequence, the ratio (I₁₃₅₅/I₁₅₅₀)/(I₁₃₇₅/I₁₅₈₀) (the affinity of hemoglobin for ligands) increases and an increase in I₁₃₇₅/I₁₁₇₂ (change in the conformation of pyrroles) is recorded. Changes in the spectra of genomic DNA are also observed at frequencies caused by stretching vibrations of primary amines (3400 cm^–1), secondary amines and hydroxyls involved in hydrogen bonding (3100 cm^–1), CH2 groups of sugar phosphates (2900 cm^–1) , vibrations of vibrational bonds between nitrogenous bases and sugars (1400 cm^–1). During IS, significant changes are observed in the spectra of genomic DNA and hemoglobin, which indicate conformational rearrangements of these molecules. In severe IS, the severity of the detected changes in the spectra of DNA and hemoglobin was maximum.