Characterization of β2-microglobulin conformational intermediates associated to different fibrillation conditions

Journal of Mass Spectrometry

Volumn 46, Issue 8, 2011, Pages 734-741

  Santambrogio, Carlo ^a   Ricagno, Stefano ^b   Sobott, Frank ^c   Colombo, Matteo ^b   Bolognesi, Martino ^b   Grandori, Rita ^a  

^a UNIVERSITY OF MILANO BICOCCA   (Italy)

^b UNIVERSITY OF MILAN   (Italy)

^c UNIVERSITY OF ANTWERP   (Belgium)

Author keywords

amyloidogenic intermediate; circular dichroism; dialysis related amyloidosis; electrospray ionisation mass spectrometry; ion mobility spectrometry

Indexed keywords

2 ,2 ,2-TRIFLUOROETHANOL; ACIDIC PH; AGGREGATION PROPENSITY; AMYLOIDOGENIC INTERMEDIATE; CONFORMATIONAL ENSEMBLE; CONFORMATIONAL INTERMEDIATES; CONFORMATIONAL PROPERTIES; DIALYSIS-RELATED AMYLOIDOSIS; ELECTROSPRAY IONIZATION MASS SPECTROMETRY; ELECTROSPRAYS; FOLDED STATE; HELICAL STRUCTURES; IN-VITRO; ION MOBILITY SPECTROMETRY; ION MOBILITY-MASS SPECTROMETRY; LIGHT CHAIN; MAJOR HISTOCOMPATIBILITY COMPLEX; NEUTRAL PH; RANDOM COIL; SECONDARY STRUCTURES; SKELETAL JOINTS; SPECIES DISTRIBUTIONS;

CIRCULAR DICHROISM SPECTROSCOPY; DIALYSIS; DICHROISM; DISEASES; ETHANOL; IONIZATION; MASS SPECTROMETRY; STRUCTURE (COMPOSITION);

ELECTROSPRAY IONIZATION;

AMYLOID; BETA 2 MICROGLOBULIN;

AMYLOIDOSIS; ARTICLE; CIRCULAR DICHROISM; DIALYSIS; ELECTROSPRAY MASS SPECTROMETRY; FLUORESCENCE SPECTROSCOPY; ION MOBILITY MASS SPECTROMETRY; JOINT; MAJOR HISTOCOMPATIBILITY COMPLEX; MASS SPECTROMETER; MASS SPECTROMETRY; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; SKELETON;

AMYLOID; AMYLOIDOSIS; BETA 2-MICROGLOBULIN; CIRCULAR DICHROISM; HUMANS; HYDROGEN-ION CONCENTRATION; PROTEIN CONFORMATION; PROTEIN FOLDING; RENAL DIALYSIS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; TRIFLUOROETHANOL;

EID: 79960550339     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.1946     Document Type: Article

References (57)

1. F. Chiti, C. M. Dobson., Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75, 333.
2. M. Fandrich, J. Meinhardt, N. Grigorieff., Structural polymorphism of Alzheimer A beta and other amyloid fibrils. Prion 2009, 3, 89.
3. D. Hamada, I. Yanagihara, K. Tsumoto., Engineering amyloidogenicity towards the development of nanofibrillar materials. Trends Biotechnol. 2004, 22, 93.
4. A. M. Morris, M. A. Watzky, R. G. Finke., Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature. Biochim. Biophys. Acta 2009, 1794, 375.
5. G. Bhak, Y. J. Choe, S. R. Paik., Mechanism of amyloidogenesis: nucleation-dependent fibrillation versus double-concentrated fibrillation. BMB Rep. 2009, 42, 541.
6. T. Ban, K. Yamaguchi, Y. Goto., Direct observation of amyloid fibril growth, propagation, and adaptation. Acc. Chem. Res. 2006, 39, 663.
7. F. Chiti, C. M. Dobson., Amyloid formation by globular proteins under native conditions. Nat. Chem. Biol. 2009, 5, 15.
8. P. A. Wearsch, P. Cresswell., The quality control of MHC class I peptide loading. Curr. Opin. Cell Biol. 2008, 20, 624.
9. M. A. Saper, P. J. Bjorkman, D. C. Wiley., Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution. J. Mol. Biol. 1991, 219, 277.
10. J. Floege, G. Ehlerding., Beta-2-microglobulin-associated amyloidosis. Nephron. 1996, 72, 9.
11. C. Menaa, E. Esser, S. M. Sprague., Beta2-microglobulin stimulates osteoclast formation. Kidney Int. 2008, 73, 1275.
12. N. M. Kad, S. L. Myers, D. P. Smith, D. A. Smith, S. E. Radford, N. H. Thompson., Hierarchical assembly of beta2-microglobulin amyloid in vitro revealed by atomic force microscopy. J. Mol. Biol. 2003, 330, 785.
13. V. J. McParland, N. M. Kad, A. P. Kalverda, A. Brown, P. Kinwin-Jones, M. G. Hunter, M. Sunde, S. E. Radford., Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro. Biochemistry 2000, 39, 8735.
14. E. Rennella, A. Corazza, S. Giorgetti, F. Fogolari, P. Viglino, R. Porcari, L. Verga, M. Stoppini, V. Bellotti, G. Esposito., Folding and fibrillogenesis: clues from beta2-microglobulin. J. Mol. Biol. 2010, 401, 286.
15. S. Yamamoto, I. Yamaguchi, K. Hasegawa, S. Tsutsumi, Y. Goto, F. Gejyo, H. Naiki., Glycosaminoglycans enhance the trifluoroethanol-induced extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH. J. Am. Soc. Nephrol. 2004, 15, 126.
16. F. Chiti, E. De Lorenzi, G. S. P. Mangione, S. Giorgetti, G. Caccialanza, C. M. Dobson, G. Merlini, G. Ramponi, V. Bellotti., A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis. J. Biol. Chem. 2001, 276, 46714.
17. A. J. Borysik, S. E. Radford, A. E. Ashcroft., Co-populated conformational ensembles of beta2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry. J. Biol. Chem. 2004, 279, 27069.
18. A. M. Smith, T. R. Jahn, A. E. Ashcroft, S. E. Radford., Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry. J. Mol. Biol. 2006, 364, 9.
19. K. Sasahara, H. Yagi, H. Naiki, Y. Goto., Heat-induced conversion of beta(2)-microglobulin and hen egg-white lysozyme into amyloid fibrils. J. Mol. Biol. 2007, 372, 981.
20. S. Yamamoto, K. Hasegawa, I. Yamaguchi, S. Tsutsumi, J. Kardos, Y. Goto, F. Gejyo, H. Naiki., Low concentrations of sodium dodecyl sulfate induce the extension of beta 2-microglobulin-related amyloid fibrils at neutral pH. Biochemistry 2004, 43, 11075.
21. C. M. Eakin, A. J. Berman, A. D. Miranker., A native to amyloidogenic transition regulated by a backbone trigger. Nat. Struct. Mol. Biol. 2006, 13, 202.
22. M. Sakata, E. Chatani, A. Kameda, K. Sakurai, H. Naiki, Y. Goto., Kinetic coupling of folding and prolyl isomerization of beta2-microglobulin studied by mutational analysis. J. Mol. Biol. 2008, 382, 1242.
23. C. M. Eakin, J. D. Knight, C. J. Morgan, M. A. Gelfand, A. D. Miranker., Formation of copper specific binding site in non-native state of beta-2-microglobulin. Biochemistry 2002, 41, 10646.
24. C. Rosano, S. Zuccotti, P. Mangione, S. Giorgetti, V. Bellotti, F. Pettirossi, A. Corazza, P. Viglino, G. Esposito, M. Bolognesi., Beta2-microglobulin H31Y variant 3D structure highlights the protein natural propensity towards intermolecular aggregation. J. Mol. Biol. 2004, 335, 1051.
25. M. F. Calabrese, C. M. Eakin, J. M. Wang, A. D. Miranker., A regulatable switch mediates self-association in an immunoglobulin fold. Nat. Struct. Mol. Biol. 2008, 15, 965.
26. T. Eichner, A. P. Kalverda, G. S. Thompson, S. W. Homans, S. E. Radford., Conformational conversion during amyloid formation at atomic resolution. Mol. Cell 2011, 41, 161.
27. G. Esposito, R. Michelutti, G. Verdone, P. Viglino, H. Hernández, C. V. Robinson, A. Amoresano, F. Dal Piaz, M. Monti, P. Pucci, P. Mangione, M. Stoppini, G. Merlini, G. Ferri, V. Bellotti., Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci. 2000, 9, 831.
28. L. M. Gierasch., How one bad protein spoils the barrel: structural details of beta(2)-microglobulin amyloidogenicity. Mol. Cell 2011, 41, 129.
29. D. P. Smith, K. Giles, R. H. Bateman, S. E. Radford, A. E. Ashcroft., Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry. J. Am. Soc. Mass Spectrom. 2007, 18, 2180.
30. G. Esposito, S. Ricagno, A. Corazza, E. Rennella, D. Gumral, M. C. Mimmi, E. Betto, C. E. Pucillo, F. Fogolari, P. Viglino, S. Raimondi, S. Giorgetti, B. Bolognesi, G. Merlini, M. Stoppini, M. Bolognesi, V. Bellotti., The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties. J. Mol. Biol. 2008, 378, 887.
31. S. Ricagno, S. Raimondi, S. Giorgetti, V. Bellotti, M. Bolognesi., Human beta-2 microglobulin W60V mutant structure: implications for stability and amyloid aggregation. Biochem. Biophys. Res. Commun. 2009, 380, 543.
32. S. Ricagno, M. Colombo, M. de Rosa, E. Sangiovanni, S. Giorgetti, S. Raimondi, V. Bellotti, M. Bolognesi., DE loop mutations affect beta-2 microglobulin stability and amyloid aggregation. Biochem. Biophys. Res. Commun. 2008, 377, 146.
33. S. E. Radford, W. S. Gosal, G. W. Platt., Towards an understanding of the structural molecular mechanism of beta(2)-microglobulin amyloid formation in vitro. Biochim. Biophys. Acta 2005, 1753, 51.
34. D. P. Smith, S. E. Radford, A. E. Ashcroft., Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry. Proc. Natl. Acad. Sci. U. S. A. 2010, 107, 6794.
35. D. P. Smith, T. W. Knapman, I. Campuzano, R. W. Malham, J. T. Berryman, S. E. Radford, A. E. Ashcroft., Deciphering drift time measurements from travelling wave ion mobility spectrometry-mass spectrometry studies. Eur. J. Mass Spectrom. 2009, 15, 113.
36. G. W. Platt, V. J. McParland, A. P. Kalverda, S. W. Homans, S. E. Radford., Dynamics in the unfolded state of beta2-microglobulin studied by NMR. J. Mol. Biol. 2005, 346, 279.
37. V. J. McParland, A. P. Kalverda, S. W. Homans, S. E. Radford., Structural properties of an amyloid precursor of beta(2)-microglobulin. Nat. Struct. Mol. Biol. 2002, 9, 326.
38. F. Fogolari, A. Corazza, N. Varini, M. Rotter, D. Gumral, L. Codutti, E. Rennella, P. Viglino, V. Bellotti, G. Esposito., Molecular dynamics simulation of beta(2)-microglobulin in denaturing and stabilizing conditions. Proteins 2010, 79, 986.
39. A. Dobo, I. A. Kaltashov., Detection of multiple protein conformational ensembles in solution via deconvolution of charge-state distributions in ESI MS. Anal. Chem. 2001, 73, 4763.
40. A. Mohimen, A. Dobo, J. K. Hoerner, I. A. Kaltashov., A chemometric approach to detection and characterization of multiple protein conformers in solution using electrospray ionization mass spectrometry. Anal. Chem. 2003, 75, 4139.
41. I. A. Kaltashov, R. R. Abzalimov., Do ionic charges in ESI MS provide useful information on macromolecular structure? J. Am. Soc. Mass Spectrom. 2008, 19, 1239.
42. A. K. Frimpong, R. R. Abzalimov, V. N. Uversky, I. A. Kaltashov., Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synuclein. Proteins 2010, 78, 714.
43. L. Testa, S. Brocca, M. Åamalikova, C. Santambrogio, L. Alberghina, R. Grandori., Electrospray ionization-mass spectrometry conformational analysis of isolated domains of an intrinsically disordered protein. Biotechnol. J. 2010, 6, 96.
44. I. A. Kaltashov, A. Mohimen., Estimates of protein surface areas in solution by electrospray ionization mass spectrometry. Anal. Chem. 2005, 77, 5370.
45. C. Santambrogio, R. Grandori., Monitoring the Tanford transition in beta-lactoglobulin by 8-anilino-1-naphthalene sulfonate and mass spectrometry. Rapid Commun. Mass Spectrom. 2008, 22, 4049.
46. V. L. Mendoza, K. Antwi, M. A. Barõn-Rodríguez, C. Blanco, R. W. Vachet., Structure of the preamyloid dimer of beta-2-microglobulin from covalent labeling and mass spectrometry. Biochemistry 2010, 49, 1522.
47. C. Uetrecht, R. J. Rose, E. van Duijn, K. Lorenzen, A. J. Heck., Ion mobility mass spectrometry of proteins and protein assemblies. Chem. Soc. Rev. 2010, 39, 1633.
48. C. S. Kaddis, J. A. Loo., Native protein MS and ion mobility large flying proteins with ESI. Anal. Chem. 2007, 79, 1778.
49. C. Santambrogio, S. Ricagno, M. Colombo, A. Barbiroli, F. Bonomi, V. Bellotti, M. Bolognesi, R. Grandori., DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded form. Protein Sci. 2010, 19, 1386.
50. G. Esposito, R. Michelutti, G. Verdone, P. Viglino, H. Hernandez, C. V. Robinson, A. Amoresano, F. Dal Piaz, M. Monti, P. Pucci, P. Mangione, M. Stoppini, G. Merlini, G. Ferri, V. Bellotti., Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibrils formation. Protein Sci. 2000, 9, 831.
51. S. M. Kelly, T. J. Jess, N. C. Prince., How to study proteins by circular dichroism. Biochim. Biophys. Acta 2005, 1751, 119.
52. K. Shiraki, K. Nishikawa, Y. Goto., Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 1995, 245, 180.
53. H. Hiramatsu, M. Lu, K. Matsuo, K. Gekko, Y. Goto, T. Kitagawa., Differences in the molecular structure of beta(2)-microglobulin between two morphologically different amyloid fibrils. Biochemistry 2010, 49, 742.
54. M. C. Kuprowski, L. Konermann., Signal response of coexisting protein conformers in electrospray mass spectrometry. Anal. Chem. 2007, 79, 2499.
55. R. Grandori, I. Matecko, N. Müller., Uncoupled analysis of secondary and tertiary protein structure by circular dichroism and electrospray ionization mass spectrometry. J. Mass Spectrom. 2002, 37, 191.
56. T. E. Creighton., Proteins-Structures and Molecular Properties, 2nd edn, Freeman W. H. & Co.: New York, 1993.
57. S. Ricagno, S. Raimondi, S. Giorgetti, V. Bellotti, M. Bolognesi., Human beta-2 microglobulin W60V mutant structure: implications for stability and amyloid aggregation. Biochem. Biophys. Res. Commun. 2009, 380, 543.