Studies on chemically modified forms of the myelin basic protein: Requirements for encephalitogenicity

Myelin-derived and putative molecular mimic peptides share structural properties in aqueous and membrane-like environments

“…Much of the early research was carried out using MBP purified from tissue [20][21][22][23][24][25]27], and more recently, recombinant MBP has also been intensively studied [29,30,48,49]. According to the current view, MBP is intrinsically disordered in solution, but folds into short helical segments upon membrane binding [87].…”

“…However, it is not known whether the self-epitopes are present in the native physiological state, or whether they form after conformational changes or denaturation caused by insults against myelinating glial cells and subsequent antigen presentation. MBP isolated from nerve tissue has been for long known for its intrinsically disordered structure and conformational changes induced by lipids [20][21][22][23][24][25][26][27]; much of this work stems from isolation of native protein from tissue, which will inevitably produce heterogeneous samples. Full-length 18.5-kDa murine MBP and the MBP72-107 peptide underwent a disordered-to-ordered transition, when transferred from an aqueous to a membranelike environment in a trifluoroethanol (TFE) titration experiment [28,29].…”