Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives

Research output: Contribution to journalArticleScientificpeer-review

Standard

Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives. / Castelletto, V.; Ryumin, P.; Cramer, R.; Hamley, I. W.; Taylor, M.; Allsop, D.; Reza, M.; Ruokolainen, J.; Arnold, T.; Hermida-Merino, D.; Garcia, C. I.; Leal, M. C.; Castaño, E.

In: Scientific Reports, Vol. 7, 43637, 08.03.2017, p. 1-12.

Research output: Contribution to journalArticleScientificpeer-review

Harvard

Castelletto, V, Ryumin, P, Cramer, R, Hamley, IW, Taylor, M, Allsop, D, Reza, M, Ruokolainen, J, Arnold, T, Hermida-Merino, D, Garcia, CI, Leal, MC & Castaño, E 2017, 'Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives' Scientific Reports, vol. 7, 43637, pp. 1-12. https://doi.org/10.1038/srep43637

APA

Castelletto, V., Ryumin, P., Cramer, R., Hamley, I. W., Taylor, M., Allsop, D., ... Castaño, E. (2017). Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives. Scientific Reports, 7, 1-12. [43637]. https://doi.org/10.1038/srep43637

Vancouver

Castelletto V, Ryumin P, Cramer R, Hamley IW, Taylor M, Allsop D et al. Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives. Scientific Reports. 2017 Mar 8;7:1-12. 43637. https://doi.org/10.1038/srep43637

Author

Castelletto, V. ; Ryumin, P. ; Cramer, R. ; Hamley, I. W. ; Taylor, M. ; Allsop, D. ; Reza, M. ; Ruokolainen, J. ; Arnold, T. ; Hermida-Merino, D. ; Garcia, C. I. ; Leal, M. C. ; Castaño, E. / Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives. In: Scientific Reports. 2017 ; Vol. 7. pp. 1-12.

Bibtex - Download

@article{e99ae9fc8cef4f3480d9cee803e557e1,
title = "Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives",
abstract = "The self-assembly of two derivatives of KLVFF, a fragment Aβ(16-20) of the amyloid beta (Aβ) peptide, is investigated and recovery of viability of neuroblastoma cells exposed to Aβ (1-42) is observed at sub-stoichiometric peptide concentrations. Fluorescence assays show that NH 2 -KLVFF-CONH 2 undergoes hydrophobic collapse and amyloid formation at the same critical aggregation concentration (cac). In contrast, NH 2 -K(Boc)LVFF-CONH 2 undergoes hydrophobic collapse at a low concentration, followed by amyloid formation at a higher cac. These findings are supported by the β-sheet features observed by FTIR. Electrospray ionization mass spectrometry indicates that NH 2 -K(Boc)LVFF-CONH 2 forms a significant population of oligomeric species above the cac. Cryo-TEM, used together with SAXS to determine fibril dimensions, shows that the length and degree of twisting of peptide fibrils seem to be influenced by the net peptide charge. Grazing incidence X-ray scattering from thin peptide films shows features of β-sheet ordering for both peptides, along with evidence for lamellar ordering of NH 2 -KLVFF-CONH 2. This work provides a comprehensive picture of the aggregation properties of these two KLVFF derivatives and shows their utility, in unaggregated form, in restoring the viability of neuroblastoma cells against Aβ-induced toxicity.",
author = "V. Castelletto and P. Ryumin and R. Cramer and Hamley, {I. W.} and M. Taylor and D. Allsop and M. Reza and J. Ruokolainen and T. Arnold and D. Hermida-Merino and Garcia, {C. I.} and Leal, {M. C.} and E. Casta{\~n}o",
year = "2017",
month = "3",
day = "8",
doi = "10.1038/srep43637",
language = "English",
volume = "7",
pages = "1--12",
journal = "Scientific Reports",
issn = "2045-2322",

}

RIS - Download

TY - JOUR

T1 - Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives

AU - Castelletto, V.

AU - Ryumin, P.

AU - Cramer, R.

AU - Hamley, I. W.

AU - Taylor, M.

AU - Allsop, D.

AU - Reza, M.

AU - Ruokolainen, J.

AU - Arnold, T.

AU - Hermida-Merino, D.

AU - Garcia, C. I.

AU - Leal, M. C.

AU - Castaño, E.

PY - 2017/3/8

Y1 - 2017/3/8

N2 - The self-assembly of two derivatives of KLVFF, a fragment Aβ(16-20) of the amyloid beta (Aβ) peptide, is investigated and recovery of viability of neuroblastoma cells exposed to Aβ (1-42) is observed at sub-stoichiometric peptide concentrations. Fluorescence assays show that NH 2 -KLVFF-CONH 2 undergoes hydrophobic collapse and amyloid formation at the same critical aggregation concentration (cac). In contrast, NH 2 -K(Boc)LVFF-CONH 2 undergoes hydrophobic collapse at a low concentration, followed by amyloid formation at a higher cac. These findings are supported by the β-sheet features observed by FTIR. Electrospray ionization mass spectrometry indicates that NH 2 -K(Boc)LVFF-CONH 2 forms a significant population of oligomeric species above the cac. Cryo-TEM, used together with SAXS to determine fibril dimensions, shows that the length and degree of twisting of peptide fibrils seem to be influenced by the net peptide charge. Grazing incidence X-ray scattering from thin peptide films shows features of β-sheet ordering for both peptides, along with evidence for lamellar ordering of NH 2 -KLVFF-CONH 2. This work provides a comprehensive picture of the aggregation properties of these two KLVFF derivatives and shows their utility, in unaggregated form, in restoring the viability of neuroblastoma cells against Aβ-induced toxicity.

AB - The self-assembly of two derivatives of KLVFF, a fragment Aβ(16-20) of the amyloid beta (Aβ) peptide, is investigated and recovery of viability of neuroblastoma cells exposed to Aβ (1-42) is observed at sub-stoichiometric peptide concentrations. Fluorescence assays show that NH 2 -KLVFF-CONH 2 undergoes hydrophobic collapse and amyloid formation at the same critical aggregation concentration (cac). In contrast, NH 2 -K(Boc)LVFF-CONH 2 undergoes hydrophobic collapse at a low concentration, followed by amyloid formation at a higher cac. These findings are supported by the β-sheet features observed by FTIR. Electrospray ionization mass spectrometry indicates that NH 2 -K(Boc)LVFF-CONH 2 forms a significant population of oligomeric species above the cac. Cryo-TEM, used together with SAXS to determine fibril dimensions, shows that the length and degree of twisting of peptide fibrils seem to be influenced by the net peptide charge. Grazing incidence X-ray scattering from thin peptide films shows features of β-sheet ordering for both peptides, along with evidence for lamellar ordering of NH 2 -KLVFF-CONH 2. This work provides a comprehensive picture of the aggregation properties of these two KLVFF derivatives and shows their utility, in unaggregated form, in restoring the viability of neuroblastoma cells against Aβ-induced toxicity.

UR - http://www.scopus.com/inward/record.url?scp=85014918980&partnerID=8YFLogxK

U2 - 10.1038/srep43637

DO - 10.1038/srep43637

M3 - Article

VL - 7

SP - 1

EP - 12

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 43637

ER -

ID: 11411447