Structure, stability, and aggregation of β-2 microglobulin mutants: Insights from a Fourier transform infrared study in solution and in the crystalline state

Biophysical Journal

Volumn 102, Issue 7, 2012, Pages 1676-1684

  Ami, Diletta ^a   Ricagno, Stefano ^b   Bolognesi, Martino ^b,c   Bellotti, Vittorio ^d,e   Doglia, Silvia Maria ^a   Natalello, Antonino ^a  

^a UNIVERSITY OF MILANO BICOCCA   (Italy)

^b UNIVERSITY OF MILAN   (Italy)

^c CNR   (Italy)

^d UNIVERSITY OF PAVIA   (Italy)

^e UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 MICROGLOBULIN; MUTANT PROTEIN;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; INFRARED SPECTROSCOPY; KINETICS; MUTATION; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; SOLUTION AND SOLUBILITY; TEMPERATURE; X RAY CRYSTALLOGRAPHY;

BETA 2-MICROGLOBULIN; CRYSTALLOGRAPHY, X-RAY; KINETICS; MODELS, MOLECULAR; MUTANT PROTEINS; MUTATION; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; SOLUTIONS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE;

EID: 84859416802     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.02.045     Document Type: Article

References (34)

1. C.H. Trinh, and D.P. Smith S.E. Radford Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties Proc. Natl. Acad. Sci. USA 99 2002 9771 9776
2. S.A. Porcelli, and R.L. Modlin The CD1 system: antigen-presenting molecules for T cell recognition of lipids and glycolipids Annu. Rev. Immunol. 17 1999 297 329
3. S. Ricagno, and S. Raimondi M. Bolognesi Human beta-2 microglobulin W60V mutant structure: implications for stability and amyloid aggregation Biochem. Biophys. Res. Commun. 380 2009 543 547
4. G. Esposito, and S. Ricagno V. Bellotti The controlling roles of Trp-60 and Trp-95 in beta2-microglobulin function, folding and amyloid aggregation properties J. Mol. Biol. 378 2008 887 897
5. S. Ricagno, and M. Colombo M. Bolognesi DE loop mutations affect beta2-microglobulin stability and amyloid aggregation Biochem. Biophys. Res. Commun. 377 2008 146 150
6. S. Azinas, and M. Colombo M. Bolognesi D-strand perturbation and amyloid propensity in beta-2 microglobulin FEBS J. 278 2011 2349 2358
7. M. Colombo, and S. Ricagno M. Bolognesi The effects of an ideal beta-turn on beta-2 microglobulin fold stability J. Biochem. 150 2011 39 47
8. M. Kihara, and E. Chatani Y. Goto Conformation of amyloid fibrils of beta2-microglobulin probed by tryptophan mutagenesis J. Biol. Chem. 281 2006 31061 31069
9. C. Santambrogio, and S. Ricagno R. Grandori DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded form Protein Sci. 19 2010 1386 1394
10. A. Barth, and C. Zscherp What vibrations tell us about proteins Q. Rev. Biophys. 35 2002 369 430
11. J.L.R. Arrondo, and F.M. Goñi Structure and dynamics of membrane proteins as studied by infrared spectroscopy Prog. Biophys. Mol. Biol. 72 1999 367 405
12. L.K. Tamm, and S.A. Tatulian Infrared spectroscopy of proteins and peptides in lipid bilayers Q. Rev. Biophys. 30 1997 365 429
13. J.M. Hadden, D. Chapman, and D.C. Lee A comparison of infrared spectra of proteins in solution and crystalline forms Biochim. Biophys. Acta 1248 1995 115 122
14. A. Natalello, and V.V. Prokorov S.M. Doglia Conformational plasticity of the Gerstmann-Sträussler-Scheinker disease peptide as indicated by its multiple aggregation pathways J. Mol. Biol. 381 2008 1349 1361
15. A.R. Pearson, and A. Mozzarelli X-ray crystallography marries spectroscopy to unveil structure and function of biological macromolecules Biochim. Biophys. Acta 1814 2011 731 733
16. P.I. Haris, and F. Severcan FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media J. Mol. Catal., B Enzym. 7 1999 207 221
17. F. Orsini, and D. Ami S.M. Doglia FT-IR microspectroscopy for microbiological studies J. Microbiol. Methods 42 2000 17 27
18. J.T. Sage, and Y. Zhang J.J. van Thor Infrared protein crystallography Biochim. Biophys. Acta 1814 2011 760 777
19. K.L.A. Chan, and L. Govada S.G. Kazarian Attenuated total reflection-FT-IR spectroscopic imaging of protein crystallization Anal. Chem. 81 2009 3769 3775
20. G. Esposito, and R. Michelutti V. Bellotti Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation Protein Sci. 9 2000 831 845
21. H. Susi, and D.M. Byler Resolution-enhanced Fourier transform infrared spectroscopy of enzymes Methods Enzymol. 130 1986 290 311
22. J. Kardos, and D. Okuno Y. Goto Structural studies reveal that the diverse morphology of beta(2)-microglobulin aggregates is a reflection of different molecular architectures Biochim. Biophys. Acta 1753 2005 108 120
23. H. Fabian, and K. Gast D. Naumann Early stages of misfolding and association of beta2-microglobulin: insights from infrared spectroscopy and dynamic light scattering Biochemistry 47 2008 6895 6906
24. S. Seshadri, R. Khurana, and A.L. Fink Fourier transform infrared spectroscopy in analysis of protein deposits Methods Enzymol. 309 1999 559 576
25. A. Natalello, and A.M. Frana M.E. Regonesi A major role for side-chain polyglutamine hydrogen bonding in irreversible ataxin-3 aggregation PLoS ONE 6 2011 e18789
26. H. Naiki, and N. Hashimoto F. Gejyo Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro Amyloid 4 1997 223 232
27. S. Yamamoto, and I. Yamaguchi H. Naiki Glycosaminoglycans enhance the trifluoroethanol-induced extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH J. Am. Soc. Nephrol. 15 2004 126 133
28. C. Santambrogio, and S. Ricagno R. Grandori Characterization of β2-microglobulin conformational intermediates associated to different fibrillation conditions J. Mass Spectrom. 46 2011 734 741
29. E. Rennella, and A. Corazza G. Esposito Folding and fibrillogenesis: clues from beta(2)- microglobulin J. Mol. Biol. 401 2010 286 297
30. M. Stefani Protein folding and misfolding on surfaces Int. J. Mol. Sci. 9 2008 2515 2542
31. M. Zhu, and P.O. Souillac A.L. Fink Surface-catalyzed amyloid fibril formation J. Biol. Chem. 277 2002 50914 50922
32. E.L. Malin, and M.H. Alaimo P.F. Fox Solution structures of casein peptides: NMR, FTIR, CD, and molecular modeling studies of alphas1-casein, 1-23 J. Protein Chem. 20 2001 391 404
33. H. Fabian, and D. Naumann H. Welfle Secondary structure of streptokinase in aqueous solution: a Fourier transform infrared spectroscopic study Biochemistry 31 1992 6532 6538
34. R. Chehín, and I. Iloro J.L. Arrondo Thermal and pH-induced conformational changes of a beta-sheet protein monitored by infrared spectroscopy Biochemistry 38 1999 1525 1530