Isoflurane's Effect on Protein Conformation as a Proposed Mechanism for Preconditioning

Figure 6

Target HSA species that are modified by MG. Our model suggests that the HSA dimer represents an isologous association of twofold symmetry with complementary binding sites indicated by squares and triangles. The nucleus for further higher-order HSA oligomerization may be a trimer [24] with a proposed screw symmetry, forming a heterologous association. While isoflurane promotes dimerization [5], it may also affect the distribution of HSA dimer subpopulations (indicated by italicized subscripts: i, j, and k). Intra- and intermolecular crosslinking by MG (as well as surface residue acetylation) may be influenced by subunit interaction and lead to cellular responses conferring preconditioning.