Conformational Change of a Synthetic Amyloid Analogue Des[Ala21,30]A42 Upon Binding to Octyl Glucoside Micelles

Overview

Journal Eur Biophys J

Specialty Biophysics

Date 1992 Jan 1

PMID 1483409

Citations 1

Authors

M Hollosi

V M Lee

H H Mantsch

Affiliations

Soon will be listed here.

Abstract

The secondary structure of a synthetic amyloid fragment des [Ala21,30]A42 was studied by circular dichroism and Fourier transformed infrared spectroscopy. Measurements were performed in trifluoroethanol/water and octyl beta-D-glucopyranoside solutions. The spectra of the peptide in trifluoroethanol indicate a high percentage of alpha-helical structure. However, in octyl glucoside, at and above the critical micelle concentration, the peptide adopts a beta-sheet conformation. Secondary structure analysis yields a predominant (> 70%) beta-sheet content. Our data suggest that the peptide backbone or polar side groups of des[Ala21,30]A42 interact with the sugar-coated surface of micelles, which promotes an alpha to beta conformational transition.

Citing Articles

Proteoglycans and other basement membrane proteins in amyloidoses.

Kisilevsky R Mol Neurobiol. 1994; 9(1-3):23-4.

PMID: 7888099 DOI: 10.1007/BF02816101.

References

Johnson Jr W . The circular dichroism of carbohydrates. Adv Carbohydr Chem Biochem. 1987; 45:73-124. View

Brunden K, Uratani Y, Cramer W . Dependence of the conformation of a colicin E1 channel-forming peptide on acidic pH and solvent polarity. J Biol Chem. 1984; 259(12):7682-7. View

Argos P, Hanei M, Garavito R . The Chou-Fasman secondary structure prediction method with an extended data base. FEBS Lett. 1978; 93(1):19-24. DOI: 10.1016/0014-5793(78)80795-9. View

KYTE J, Doolittle R . A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982; 157(1):105-32. DOI: 10.1016/0022-2836(82)90515-0. View

Otvos Jr L, ELEKES I, Lee V . Solid-phase synthesis of phosphopeptides. Int J Pept Protein Res. 1989; 34(2):129-33. DOI: 10.1111/j.1399-3011.1989.tb01501.x. View

Weidemann A, Konig G, Bunke D, Fischer P, Salbaum J, Masters C . Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell. 1989; 57(1):115-26. DOI: 10.1016/0092-8674(89)90177-3. View

Urry D, Masotti L, Krivacic J . Circular dichroism of biological membranes. I. Mitochondria and red blood cell ghosts. Biochim Biophys Acta. 1971; 241(2):600-12. DOI: 10.1016/0005-2736(71)90058-7. View

Hilbich C, Reed J, Masters C, Beyreuther K . Human and rodent sequence analogs of Alzheimer's amyloid beta A4 share similar properties and can be solubilized in buffers of pH 7.4. Eur J Biochem. 1991; 201(1):61-9. DOI: 10.1111/j.1432-1033.1991.tb16256.x. View

Andreu J . Interaction of tubulin with non-denaturing amphiphiles. EMBO J. 1982; 1(9):1105-10. PMC: 553170. DOI: 10.1002/j.1460-2075.1982.tb01304.x. View

10.

Eisenberg D, Schwarz E, Komaromy M, Wall R . Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J Mol Biol. 1984; 179(1):125-42. DOI: 10.1016/0022-2836(84)90309-7. View

11.

Dyrks T, Weidemann A, Multhaup G, Salbaum J, Lemaire H, Kang J . Identification, transmembrane orientation and biogenesis of the amyloid A4 precursor of Alzheimer's disease. EMBO J. 1988; 7(4):949-57. PMC: 454420. DOI: 10.1002/j.1460-2075.1988.tb02900.x. View

12.

Surewicz W, Mantsch H . New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim Biophys Acta. 1988; 952(2):115-30. DOI: 10.1016/0167-4838(88)90107-0. View

13.

Werner P, Reithmeier R . Molecular characterization of the human erythrocyte anion transport protein in octyl glucoside. Biochemistry. 1985; 24(23):6375-81. DOI: 10.1021/bi00344a009. View

14.

Hollosi M, Otvos Jr L, Kajtar J, Percel A, Lee V . Is amyloid deposition in Alzheimer's disease preceded by an environment-induced double conformational transition?. Pept Res. 1989; 2(1):109-13. View

15.

Hilbich C, Reed J, Masters C, Beyreuther K . Aggregation and secondary structure of synthetic amyloid beta A4 peptides of Alzheimer's disease. J Mol Biol. 1991; 218(1):149-63. DOI: 10.1016/0022-2836(91)90881-6. View

16.

Krimm S, Bandekar J . Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv Protein Chem. 1986; 38:181-364. DOI: 10.1016/s0065-3233(08)60528-8. View

17.

Jackson M, Mantsch H . Beware of proteins in DMSO. Biochim Biophys Acta. 1991; 1078(2):231-5. DOI: 10.1016/0167-4838(91)90563-f. View

18.

Barrow C, Yasuda A, Kenny P, Zagorski M . Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease. Analysis of circular dichroism spectra. J Mol Biol. 1992; 225(4):1075-93. DOI: 10.1016/0022-2836(92)90106-t. View

19.

Visser L, BLOUT E . Elastase. II. Optical properties and the effects of sodium dodecyl sulfate. Biochemistry. 1971; 10(5):743-52. DOI: 10.1021/bi00781a004. View

20.

Fraser P, Nguyen J, Surewicz W, Kirschner D . pH-dependent structural transitions of Alzheimer amyloid peptides. Biophys J. 1991; 60(5):1190-201. PMC: 1260174. DOI: 10.1016/S0006-3495(91)82154-3. View