Engineering peptides and proteins that undergo α-to-β transitions

Current Opinion in Structural Biology

Volumn 7, Issue 4, 1997, Pages 501-508

  Mihara, Hisakazu ^a   Takahashi, Yuta ^a  

^a Fac Biosci Biotech   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; PRION PROTEIN; PROTEIN;

ALPHA HELIX; CONFORMATIONAL TRANSITION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; REVIEW;

EID: 0030864812     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80113-3     Document Type: Article

References (56)

1. Taubes G. Misfolding the way to diseases. of special interest Science. 271:1996;1493-1495 This news article summarizes the importance and implications of misfolding (conformational transition) and aggregation of polypeptides in protein inclusion bodies and in disease-related proteins such as β-amyloid and PrP.
2. Kelly JW. Alternative conformations of amyloidogenic proteins govern their behavior. of outstanding interest Curr Opin Struct Biol. 6:1996;11-17 This review demonstrates the importance of conformational changes during amyloid formation for various amyloidogenic proteins, including transthyretin.
3. Forloni G, Tagliavini F, Bugiani O, Salmona M. Amyloid in Alzheimer's disease and prion-related encephalopathies: studies with synthetic peptides. of outstanding interest Prog Neurobiol. 49:1996;287-315 This review summarizes and compares data obtained with β-amyloid and prion peptides and analyzes the significance in terms of amyloidogenic proteins and neurodegeneration.
4. Prusiner SB. Transgenetics of prion diseases. of special interest Curr Top Microbiol Immunol. 206:1996;275-304 This review summarizes the genetic studies on prion diseases and proposes a model for the replication of prions.
5. Wetzel R. For protein misassembly, it's the 'I' decade. of special interest Cell. 86:1996;699-702 This minireview describes the general significance of folding intermediates for protein misassembly including amyloid proteins and inclusion bodies.
6. Bychkova VE, Ptitsyn OB. Folding intermediates are involved in genetic diseases? FEBS Lett. 359:1995;6-8.
7. Speed MA, Wang DIC, King J. Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body. of special interest Nat Biotechnol. 14:1996;1283-1287 The aggregation of virus proteins P22 tailspike and P22 coat protein occurs by the specific interaction of folding intermediates, providing a rationale for recovering relatively pure protein from the inclusion body.
8. Kuwajima K. Stopped-flow circular dichroism. of special interest Fasman GD. Circular Dichroism and the Conformational Analysis of Biomolecules. 1996;159-182 Plenum, New York, This chapter summarizes the application of kinetic CD measurements to the recent studies on protein folding in a protein that contains an α-to-β transition such as β-lactoglobulin.
9. Betz SF, Raleigh DP, DeGrado WF. De novo protein design: from molten globules to native-like states. Curr Opin Struct Biol. 3:1993;601-610.
10. Betz JW, Bryson JW, DeGrado WF. Native-like and structurally characterized designed α-helical bundles. Curr Opin Struct Biol. 5:1995;457-463.
11. Lansbury PT Jr, Caughey B. The double life of the prion protein. of special interest Curr Biol. 6:1996;914-916 This minireview describes the infection model of prion proteins being the protein-only agent.
12. Sc and proposes the heterodimer model for prion replication.
13. Huang Z, Prusiner SB, Cohen FE. Scrapie prions: a three-dimensional model of an infectious fragment. Fold Des. 1:1995;13-19. [Published erratum appears in Fold Des 1995, 1:406].
14. Mehlhorn I, Groth D, Stöckel J, Moffat B, Reilly D, Yansura D, Willett WS, Baldwin M, Fletterick R, Cohen FE, et al. High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. of special interest Biochemistry. 35:1996;5528-5537 The expression and purification methods of PrP(90-231) are described, and the CD and FTIR spectra of its reduced (β sheet) and refolded (α helix) forms are provided.
15. Nguyen J, Baldwin MA, Cohen FE, Prusiner SB. Prion protein peptides induce α-helix to β-sheet conformational transitions. Biochemistry. 34:1995;4186-4192.
16. 13C-labeled H1(109-122) peptide indicates that it can fold into both α-helical and β-sheet conformations in solid state.
17. Zhang H, Kaneko K, Nguyen JT, Livshits TL, Baldwin MA, Cohen FE, James TL, Prusiner SB. Conformational transitions in peptides containing two putative α-helices of the prion protein. J Mol Biol. 250:1995;514-526.
18. Nguyen JT, Inouye H, Baldwin MA, Fletterick RJ, Cohen FE, Prusiner SB, Kirschner DA. X-ray diffraction of scrapie prion rods and PrP peptides. J Mol Biol. 252:1995;412-422.
19. Kaneko K, Peretz D, Pan KM, Blochberger TC, Wille H, Gabizon R, Griffith OH, Cohen FE, Baldwin MA, Prusiner SB. Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform. Proc Natl Acad Sci USA. 92:1995;11160-11164.
20. Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wüthrich K. NMR structure of the mouse prion protein domain PrP(121-231). of outstanding interest Nature. 382:1996;180-182 The NMR structure of PrP(121-231) in water shows the presence of a short two-stranded antiparallel β sheet and three β helices, which contrasts with the predicted structure.
21. Sc.
22. Caughey B, Kocisko DA, Raymond GJ, Lansbury PT Jr. Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state. Chem Biol. 2:1995;807-817.
23. Sc.
24. Sc is presented.
25. Lansbury PT Jr, Costa PR, Griffiths JM, Simon EJ, Auger M, Halverson KJ, Kocisko DA, Hendsch ZS, Ashburn TT, Spencer RGS, et al. Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nat Struct Biol. 2:1995;990-998.
26. Sticht H, Bayer P, Willbold D, Dames S, Hilbich C, Beyreuther K, Frank RW, Rösch P. Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease. Eur J Biochem. 233:1995;293-298.
27. 1H NMR of Aβ amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence. Biochemistry. 34:1995;5191-5200.
28. Jayawickrama D, Zink S, Vander Velde D, Effiong RI, Larive CK. Conformational analysis of the β-amyloid peptide fragment, β(12-28). J Biomol Struct Dyn. 13:1995;229-244.
29. Kohno T, Kobayashi K, Maeda T, Sato K, Takashima A. Three-dimensional structures of the amyloid β peptide (25-35) in membrane-mimicking environment. of special interest Biochemistry. 35:1996;16094-16104 This paper reports that Aβ(25-35) folds into α helix in micellar environments as determined by NMR.
30. Wood SJ, Wetzel R, Martin JD, Hurle MR. Prolines and amyloidogenecity in fragments of the Alzheimer's peptide β/A4. Biochemistry. 34:1995;724-730.
31. Esler WP, Stimson ER, Ghilardi JR, Lu YA, Felix AM, Vinters HV, Mantyh PW, Lee JP, Maggio JE. Point substitution in the central hydrophobic cluster of a human β-amyloid congener disrupts peptide folding and abolishes plaque competence. of outstanding interest Biochemistry. 35:1996;13914-13921 The authors argue that the central region of Aβ is an active congener of human β-amyloid and propose the importance of the Leu-Val-Phe-Phe-Ala (17-21) sequence for drug design.
32. Soto C, Kindy MS, Baumann M, Frangione B. Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation. of outstanding interest Biochem Biophys Res Commun. 226:1996;672-680 A designed 11-residue peptide corresponding to Aβ(15-25) with three proline residues inhibits the fibril formation of full length Aβ.
33. Tjernberg LO, Naslund J, Lindqvist F, Johansson J, Karlstrom AR, Thyberg J, Terenius L, Nordstedt C. Arrest of β-amyloid fibril formation by a pentapeptide ligand. of outstanding interest J Biol Chem. 271:1996;8545-8548 Peptides containing Aβ(16-20) can bind to Aβ(1-40) and prevent its assembly into amyloid fibrils.
34. Shen CL, Murphy RM. Solvent effects on self-assembly of β-amyloid peptide. Biophys J. 69:1995;640-651.
35. Soto C, Castano EM. The conformation of Alzheimer's β peptide determines the rate of amyloid formation and its resistance to proteolysis. Biochem J. 314:1996;701-707.
36. Soto C, Castano EM, Kumar RA, Beavis RC, Frangione B. Fibrillogenesis of synthetic amyloid-β peptides is dependent on their initial secondary structure. Neurosci Lett. 200:1995;105-108.
37. Sato K, Wakamiya A, Maeda T, Noguchi K, Takashima A, Imahori K. Correlation among secondary structure, amyloid precursor protein accumulation, and neurotoxicity of amyloid β(25-35) peptide as analyzed by single alanine substitution. J Biochem. 118:1995;1108-1111.
38. Salomon AR, Marcinowski KJ, Friedland RP, Zagorski MG. Nicotine inhibits amyloid formation by the β-peptide. of outstanding interest Biochemistry. 35:1996;13568-13578 The authors report that nicotine prevents the Aβ(1-42) peptide from precipitating as an amyloid-like deposit and argue the presence of an α-to-β transition mechanism in pathogenesis of Alzheimer's disease.
39. Wood SJ, MacKenzie L, Maleeff B, Hurle MR, Wetzel R. Selective inhibition of Aβ fibril formation. of special interest J Biol Chem. 271:1996;4086-4092 A detergent, hexadecyl-N-methylpireridinium bromide, inhibits Aβ fibril formation in a 1:1 stoichiometry but does not inhibit fibrillogenesis by other amyloidogenic proteins. The detergent contains a cyclic ammonium structure similar to nicotine.
40. Schenck HL, Dado GP, Gellman SH. Redox-triggered secondary structure changes in the aggregated states of a designed methionine-rich peptide. of outstanding interest J Am Chem Soc. 118:1996;12487-12494 The model peptide designed to have an amphiphilic character undergoes an α-to-β transition when the introduced hydrophobic methionine residues are oxidized to hydrophilic methionine sulfoxide and methionine sulfone residues. The peptide is designed skifully using both the amphiphilic α-helix and β-strand character. Interestingly, there are some methionine residues in the hydrophobic region of prion protein and Aβ.
41. Cerpa R, Cohen FE, Kuntz ID. Conformational switching in designed peptides: the helix/sheet transition. of special interest Fold Des. 1:1996;91-101 The α-β transitions of designed peptides are described with respect to solution conditions including pH, NaCl concentration, temperature, and peptide concentration.
42. Fukushima Y. Sequence effects on helix-sheet conformational transitions of designed amphiphilic peptides. Bull Chem Soc Japan. 69:1996;701-708.
43. Choo DW, Schneider JP, Graciani NR, Kelly JW. Nucleated antiparallel β-sheet that folds and undergoes self-assembly: a template promoted folding strategy toward controlled molecular architectures. of outstanding interest Macromolecules. 29:1996;355-366 A series of designed peptides that have a hydrophobic template, dibenzofuran, fold in β sheets, and the hydrophobic clustering initiates the formation of fibrils similar to amyloid peptides.
44. Hamada D, Segawa S, Goto Y. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. of outstanding interest Nat Struct Biol. 3:1996;868-873 An intermediate state of a β-sheet protein, β-lactoglobulin, generated using TFE or guanidine hydrochloride is highly α-helical. The kinetic study of the refolding suggests a nonhierarchical folding mechanism via α-to-β transitions of secondary structures.
45. Kuwajima K, Yamaya H, Sugai S. The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy. of outstanding interest J Mol Biol. 264:1996;806-822 The burst-phase intermediate of β-lactoglobulin is classified as belonging to the same species as the molten globule state. The non-native α-helices in the burst-phase intermediate may be formed in immature parts of the protein that have local α-helical propensities.
46. Kuroda Y, Hamada D, Tanaka T, Goto Y. High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy. of outstanding interest Fold Des. 1:1996;255-263 The peptide fragments corresponding to the β strands and α helices in β-lactoglobulin have an α-helical propensity in solution, which supports α-to-β transitions and the nonhierarchical mechanism of folding.
47. Hamada D, Kuroda Y, Tanaka T, Goto Y. High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein. J Mol Biol. 254:1995;737-746.
48. Narhi LO, Philo JS, Li T, Zhang M, Samal B, Arakawa T. Induction of α-helix in the β-sheet protein tumor necrosis factor-α: thermal- and trifluoroethanol-induced denaturation at neutral pH. of special interest Biochemistry. 35:1996;11447-11453 An α-to-β transition, similar to that of β-lactoglobulin, is observed for tumor necrosis factor-α using an increase in temperature and the addition of TFE.
49. Narhi LO, Philo JS, Li T, Zhang M, Samal B, Arakawa T. Induction of α-helix in the β-sheet protein tumor necrosis factor-α: acid-induced denaturation. of special interest Biochemistry. 35:1996;11454-11460 An β-to-β transition, similar to that of β-lactoglobulin, is observed for tumor necrosis factor-α using a change of pH.
50. Minor DL Jr, Kim PS. Context-dependent secondary structure formation of a designed protein sequence. of outstanding interest Nature. 380:1996;730-734 An 11-residue peptide is designed with a sequence that is a hybrid mixture between a β sheet and an α helix in the immunoglobulin-binding domain of protein G. The peptide is called a 'chameleon' because it folds in a β sheet when inserted at the β-sheet position and in an α helix at the α-helical position of the protein. The chameleon property is characterized using NMR.
51. Perutz MF. Mutations make enzyme polymerize. of special interest Nature. 385:1997;773-775 This review describes the implications of the chameleon character of the α-to-β transitional fragments in amyloidogenic proteins such as prions and mutated lysozymes.
52. Booth DR, Sunde M, Bellotti V, Robinson CV, Hutchinson WL, Fraser PE, Hawkins PN, Dobson CM, Radford SE, Blake CCF, Pepys MB. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. of outstanding interest Nature. 385:1997;787-793 The lle56→Thr and Asp67→His mutants of human lysozyme have a similar structure in the crystal form, but solution studies of these variants reveal that the instability of the mutant conformations correlates with the amyloidogenesis associated with α-to-β transitions. The properties of the mutant structures are characterized using the crystal structures, FTIR, CD, fluorescence, and denaturation studies.
53. Helms LR, Wetzel R. Specificity of abnormal assembly in immunoglobulin light chain deposition disease and amyloidosis. of outstanding interest J Mol Biol. 257:1996;77-86 Point mutations (Arg61→Asn and Asp82→lle) of the variable domain of the immunoglobulin light chain destabilize the domain conformation by disrupting the Arg61 - Asp82 salt bridge and render it susceptible to aggregate formation. The two mutants, however, deposit aggregates with different morphology.
54. McCutchen SL, Lai Z, Miroy GJ, Kelly JW, Colon W. Comparison of lethal and nonlethal transthyretin variants and their relationship of amyloid diseases. Biochemistry. 34:1995;13527-13536.
55. Lai Z, Colon W, Kelly JW. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. of outstanding interest Biochemistry. 35:1996;6470-6482 Acid conditions render the tetrameric transthyretin as a dissociated monomer, which is an intermediate of the amyloidosis. The acid denaturation pathway is examined in order to characterize the intermediate state.
56. Takahashi Y, Ueno A, Mihara H. Design and synthesis of peptide misfolding from α to β structure and regulation by β-cyclodextrin as mini-molecular chaperone. of outstanding interest Kitada C. Peptide Chemistry 1996. 1997;409-412 Protein Research Foundation, Osaka, The design and synthesis of α-to-β transitional peptides using hydrophobic defects at the N termini such as 1-adamantanecarbonyl is described. The α-to-β transitions are inhibited with an artificial molecular chaperone, β-cyclodextrin, which captures the defects in its hydrophobic cavity.