Probing the Role of Aromatic Residues in the Self-assembly of Aβ(16-22) in Fluorinated Alcohols and Their Aqueous Mixtures

Overview

Journal Biochem Biophys Rep

Specialty Biochemistry

Date 2017 Nov 11

PMID 29124140

Citations 6

Authors

Sanjai Kumar Pachahara

Ramakrishnan Nagaraj

Affiliations

Soon will be listed here.

Abstract

The Aβ(16-22) sequence KLVFFAE spans the hydrophobic core of the Aβ peptide and plays an important role in its self-assembly. Apart from forming amyloid fibrils, Aβ(16-22) can self-associate into highly ordered nanotubes and ribbon-like structures depending on the composition of solvent used for dissolution. The Aβ(16-22) sequence which has FF at the 19th and 20th positions would be a good model to investigate peptide self-assembly in the context of aromatic interactions. In this study, self-assembly of Aβ(16-22) and its aromatic analogs obtained by replacement of F19, F20 or both by Y or W was examined after dissolution in fluorinated alcohols and their aqueous mixtures in solvent cluster forming conditions. The results indicate that the presence of aromatic residues Y and W and their position in the sequence plays an important role in self-assembly. We observe the formation of amyloid fibrils and other self-assembled structures such as spheres, rings and beads. Our results indicate that 20% HFIP is more favourable for amyloid fibril formation as compared to 20% TFE, when F is replaced with Y or W. The dissolution of peptides in DMSO followed by evaporation of solvent and dissolution in water appears to greatly influence peptide conformation, morphology and cross-β content of self-assembled structures. Our study shows that positioning of aromatic residues F, Y and W have an important role in directing self-assembly of the peptides.

Citing Articles

Trifluoroacetic Acid as a Molecular Probe for the Dense Phase in Liquid-Liquid Phase-Separating Peptide Systems.

Lim J, Chin S, Miserez A, Xue K, Pervushin K Anal Chem. 2024; 97(1):166-174.

PMID: 39710972 PMC: 11740181. DOI: 10.1021/acs.analchem.4c03444.

Nonperturbative Fluorogenic Labeling of Immunophilins Enables the Wash-free Detection of Immunosuppressants.

Bertolini M, Mendive-Tapia L, Ghashghaei O, Reese A, Lochenie C, Schoepf A ACS Cent Sci. 2024; 10(5):969-977.

PMID: 38799658 PMC: 11117681. DOI: 10.1021/acscentsci.3c01590.

designed aliphatic and aromatic peptides assemble into amyloid-like cytotoxic supramolecular nanofibrils.

Samui S, Biswas S, Basak S, Ghosh S, Muniyappa K, Naskar J RSC Adv. 2024; 14(7):4382-4388.

PMID: 38304566 PMC: 10831423. DOI: 10.1039/d3ra07869h.

Fluorinated peptide biomaterials.

Sloand J, Miller M, Medina S Pept Sci (Hoboken). 2021; 113(2).

PMID: 34541446 PMC: 8448251. DOI: 10.1002/pep2.24184.

Volatile Anesthetic Sevoflurane Precursor 1,1,1,3,3,3-Hexafluoro-2-Propanol (HFIP) Exerts an Anti-Prion Activity in Prion-Infected Culture Cells.

Shimizu T, Nogami E, Ito Y, Morikawa K, Nagane M, Yamashita T Neurochem Res. 2021; 46(8):2056-2065.

PMID: 34043140 PMC: 8254714. DOI: 10.1007/s11064-021-03344-8.

References

McGaughey G, Gagne M, Rappe A . pi-Stacking interactions. Alive and well in proteins. J Biol Chem. 1998; 273(25):15458-63. DOI: 10.1074/jbc.273.25.15458. View

Tatko C, Waters M . Selective aromatic interactions in beta-hairpin peptides. J Am Chem Soc. 2002; 124(32):9372-3. DOI: 10.1021/ja0262481. View

Childers W, Anthony N, Mehta A, Berland K, Lynn D . Phase networks of cross-β peptide assemblies. Langmuir. 2012; 28(15):6386-95. DOI: 10.1021/la300143j. View

Park J, Kahng B, Hwang W . Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine. PLoS Comput Biol. 2009; 5(9):e1000492. PMC: 2723932. DOI: 10.1371/journal.pcbi.1000492. View

Huggins K, Bisaglia M, Bubacco L, Tatarek-Nossol M, Kapurniotu A, Andersen N . Designed hairpin peptides interfere with amyloidogenesis pathways: fibril formation and cytotoxicity inhibition, interception of the preamyloid state. Biochemistry. 2011; 50(38):8202-12. PMC: 3177973. DOI: 10.1021/bi200760h. View

Rajan R, Balaram P . A model for the interaction of trifluoroethanol with peptides and proteins. Int J Pept Protein Res. 1996; 48(4):328-36. DOI: 10.1111/j.1399-3011.1996.tb00849.x. View

Eidenschink L, Kier B, Andersen N . Determinants of fold stabilizing aromatic-aromatic interactions in short peptides. Adv Exp Med Biol. 2009; 611:73-4. PMC: 3816201. DOI: 10.1007/978-0-387-73657-0_32. View

Serrano L, Bycroft M, Fersht A . Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles. J Mol Biol. 1991; 218(2):465-75. DOI: 10.1016/0022-2836(91)90725-l. View

Johnson R, Hecht K, Deber C . Aromatic and cation-pi interactions enhance helix-helix association in a membrane environment. Biochemistry. 2007; 46(32):9208-14. DOI: 10.1021/bi7008773. View

10.

Naskar J, Drew M, Deb I, Das S, Banerjee A . Water-soluble tripeptide Abeta (9-11) forms amyloid-like fibrils and exhibits neurotoxicity. Org Lett. 2008; 10(13):2625-8. DOI: 10.1021/ol8007217. View

11.

Ladokhin A, Selsted M, White S . CD spectra of indolicidin antimicrobial peptides suggest turns, not polyproline helix. Biochemistry. 1999; 38(38):12313-9. DOI: 10.1021/bi9907936. View

12.

Nichols M, Moss M, Reed D, Cratic-McDaniel S, Hoh J, Rosenberry T . Amyloid-beta protofibrils differ from amyloid-beta aggregates induced in dilute hexafluoroisopropanol in stability and morphology. J Biol Chem. 2004; 280(4):2471-80. DOI: 10.1074/jbc.M410553200. View

13.

Jones S, Manning J, Kad N, Radford S . Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro. J Mol Biol. 2002; 325(2):249-57. DOI: 10.1016/s0022-2836(02)01227-5. View

14.

Westermark G, Engstrom U, Westermark P . The N-terminal segment of protein AA determines its fibrillogenic property. Biochem Biophys Res Commun. 1992; 182(1):27-33. DOI: 10.1016/s0006-291x(05)80107-x. View

15.

Mehta A, Lu K, Childers W, Liang Y, Dublin S, Dong J . Facial symmetry in protein self-assembly. J Am Chem Soc. 2008; 130(30):9829-35. DOI: 10.1021/ja801511n. View

16.

Castelletto V, Hamley I, Cenker C, Olsson U . Influence of salt on the self-assembly of two model amyloid heptapeptides. J Phys Chem B. 2010; 114(23):8002-8. DOI: 10.1021/jp102744g. View

17.

Padrick S, Miranker A . Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis. Biochemistry. 2002; 41(14):4694-703. DOI: 10.1021/bi0160462. View

18.

Thomas A, Meurisse R, Charloteaux B, Brasseur R . Aromatic side-chain interactions in proteins. I. Main structural features. Proteins. 2002; 48(4):628-34. DOI: 10.1002/prot.10190. View

19.

Espinoza-Fonseca L, Garcia-Machorro J . Aromatic-aromatic interactions in the formation of the MDM2-p53 complex. Biochem Biophys Res Commun. 2008; 370(4):547-51. DOI: 10.1016/j.bbrc.2008.03.053. View

20.

Yamaguchi K, Naiki H, Goto Y . Mechanism by which the amyloid-like fibrils of a beta 2-microglobulin fragment are induced by fluorine-substituted alcohols. J Mol Biol. 2006; 363(1):279-88. DOI: 10.1016/j.jmb.2006.08.030. View