TAILIEUCHUNG - Báo cáo khoa học: Variants of b2-microglobulin cleaved at lysine-58 retain the main conformational features of the native protein but are more conformationally heterogeneous and unstable at physiological temperature

Cleavage of the small amyloidogenic proteinb2-microglobulin after lysine-58 renders it more prone to unfolding and aggregation. This is important for dialysis-related b2 -microglobulin amyloidosis, since elevated levels of cleaved b2-microglobulin may be found in the circulation of dialysis patients. | ềFEBS Journal Variants of b2-microglobulin cleaved at lysine-58 retain the main conformational features of the native protein but are more conformationally heterogeneous and unstable at physiological temperature Maria C. Mimmi1 Thomas J. D. J0rgensen2 Fabio Pettirossi1 Alessandra Corazza1 Paolo Viglino1 Gennaro Esposito1 Ersilia De Lorenzi3 Sofia Giorgetti4 Mette Pries5 Dorthe B. Corlin6 Mogens H. Nissen5 and Niels H. H. Heegaard6 1 Dipartimento di Scienze e Tecnologie Biomediche and MATI Centre of Excellence University of Udine Italy 2 Department of Biochemistry and Molecular Biology University of Southern Denmark Odense Denmark 3 Department of PharmaceuticalChemistry Schoolof Pharmacy University of Pavia Italy 4 Department of Biochemistry Schoolof Pharmacy University of Pavia and Biotechnology Laboratories IRCCS Policlinico San Matteo Pavia Italy 5 Institute of MedicalAnatomy University of Copenhagen Denmark 6 Department of Autoimmunology Statens Serum Institut Copenhagen Denmark Keywords amyloidosis cleaved p2-microglobulin human p2-microglobulin NMR protein conformation Correspondence N. Heegaard Department of Autoimmunology Statens Serum Institut 81 536 Artillerivej 5 DK-2300 Copenhagen S Denmark Fax 45 32683876 Tel 45 32683378 E-mail nhe@ Received 31 January 2006 accepted 31 March 2006 doi Cleavage of the small amyloidogenic protein p2-microglobulin after lysine-58 renders it more prone to unfolding and aggregation. This is important for dialysis-related p2-microglobulin amyloidosis since elevated levels of cleaved b2-microglobulin may be found in the circulation of dialysis patients. However the solution structures of these cleaved b2-microglobulin variants have not yet been assessed using single-residue techniques. We here use such methods to examine b2-microglobulin cleaved after lysine-58 and the further processed variant found in vivo from which lysine-58 is removed. We find that the solution stability of both .

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