Interaction between 1-pyrenesulfonic acid and albumin: Moving inside the protein.

摘要: Abstract Due to the high sensitivity alterations in microenvironment polarity of macromolecules, pyrene and its derivatives have long been applied biosciences. Human serum albumin (HSA), besides numerous physiological functions, is main responsible by transport endogenous exogenous compounds circulatory system. Here, a comprehensive study was carry out understand interaction between HSA derivative 1-pyrenesulfonic acid (PMS), which showed singular behaviour when bound this protein. The complexation PMS with studied steady state, time-resolved anisotropy fluorescence, induction circular dichroism (ICD) molecular docking. fluorescence quenching abnormal, being stronger at lower concentration quencher. Similar obtained measuring ICD signal lifetime complexed HSA. displacement site-specific drugs that probe occupied both sites, but higher affinity for site II. movement these binding sites abnormal effect. Using holo (PDB: ID 1A06) apo 1E7A) structures, experimental results were corroborated docking simulation. spectroscopic related different regions into protein can be traced alteration signals. These findings bring new point view about use characterize ligands.