Home > Research > Publications & Outputs > Retro-inverso peptide inhibitor nanoparticles a...

Research

Associated organisational unit

Electronic data

  • Nanomedicine (in press)

    Rights statement: This is the author’s version of a work that was accepted for publication in Nanomedicine. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Nanomedicine, 13, 2, 2017 DOI: 10.1016/j.nano.2016.10.006

    Accepted author manuscript, 1.16 MB, PDF document

    Available under license: CC BY-NC-ND: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License

Links

Text available via DOI:

Keywords

View graph of relations

Retro-inverso peptide inhibitor nanoparticles as potent inhibitors of aggregation of the Alzheimer’s Aβ peptide

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Published

Standard

Retro-inverso peptide inhibitor nanoparticles as potent inhibitors of aggregation of the Alzheimer’s Aβ peptide. / Gregori, Maria; Taylor, Mark Neville; Salvati, Elisa et al.
In: Nanomedicine: Nanotechnology, Biology, and Medicine, Vol. 13, No. 2, 02.2017, p. 723-732.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Gregori, M, Taylor, MN, Salvati, E, Re, F, Mancini, S, Balducci, C, Forloni, G, Zambelli, V, Sesana, S, Michael, M, Michail, C, Kolosov, OV, Tinker-Mill, CL, Sherer, M, Harris, S, Fullwood, NJ, Masserini, M & Allsop, D 2017, 'Retro-inverso peptide inhibitor nanoparticles as potent inhibitors of aggregation of the Alzheimer’s Aβ peptide', Nanomedicine: Nanotechnology, Biology, and Medicine, vol. 13, no. 2, pp. 723-732. https://doi.org/10.1016/j.nano.2016.10.006

APA

Gregori, M., Taylor, M. N., Salvati, E., Re, F., Mancini, S., Balducci, C., Forloni, G., Zambelli, V., Sesana, S., Michael, M., Michail, C., Kolosov, O. V., Tinker-Mill, C. L., Sherer, M., Harris, S., Fullwood, N. J., Masserini, M., & Allsop, D. (2017). Retro-inverso peptide inhibitor nanoparticles as potent inhibitors of aggregation of the Alzheimer’s Aβ peptide. Nanomedicine: Nanotechnology, Biology, and Medicine, 13(2), 723-732. https://doi.org/10.1016/j.nano.2016.10.006

Vancouver

Gregori M, Taylor MN, Salvati E, Re F, Mancini S, Balducci C et al. Retro-inverso peptide inhibitor nanoparticles as potent inhibitors of aggregation of the Alzheimer’s Aβ peptide. Nanomedicine: Nanotechnology, Biology, and Medicine. 2017 Feb;13(2):723-732. Epub 2016 Oct 19. doi: 10.1016/j.nano.2016.10.006

Author

Gregori, Maria ; Taylor, Mark Neville ; Salvati, Elisa et al. / Retro-inverso peptide inhibitor nanoparticles as potent inhibitors of aggregation of the Alzheimer’s Aβ peptide. In: Nanomedicine: Nanotechnology, Biology, and Medicine. 2017 ; Vol. 13, No. 2. pp. 723-732.

Bibtex

@article{7bfd363285c84304b66fc0b7096a54f6,
title = "Retro-inverso peptide inhibitor nanoparticles as potent inhibitors of aggregation of the Alzheimer{\textquoteright}s Aβ peptide",
abstract = "Aggregation of Amyloid-β peptide (Aβ) is a key event in the pathogenesis of Alzheimer{\textquoteright}s disease (AD). We investigated the effects of nanoliposomes decorated with the retro-inverso peptide RI-OR2-TAT (Ac-rGffvlkGrrrrqrrkkrGy-NH2) on the aggregation and toxicity of Aβ. Remarkably low concentrations of these peptide inhibitor nanoparticles (PINPs) were required to inhibit the formation of Aβ oligomers and fibrils in vitro, with 50% inhibition occurring at a molar ratio of ~1:2000 of liposome-bound RI-OR2-TAT to Aβ. PINPs also bound to Aβ with high affinity (Kd = 13.2 - 50 nM), rescued SHSY-5Y cells from the toxic effect of pre-aggregated Aβ, crossed an in vitro blood-brain-barrier model (hCMEC/D3 cell monolayer), entered the brains of C57/BL6 mice, and protected against memory loss in APPSWE transgenic mice in a novel object recognition test. As the most potent aggregation inhibitor that we have tested so far, we propose to develop PINPs as a potential disease-modifying treatment for AD.",
keywords = "Alzheimer{\textquoteright}s disease, liposomes, retro-inverso peptide, β-amyloid, oligomer",
author = "Maria Gregori and Taylor, {Mark Neville} and Elisa Salvati and Francesca Re and Simona Mancini and Claudia Balducci and Gianluigi Forloni and Vanessa Zambelli and Silvia Sesana and Maria Michael and Christos Michail and Kolosov, {Oleg Victor} and Tinker-Mill, {Claire Louisa} and Mike Sherer and Stephen Harris and Fullwood, {Nigel James} and Massimo Masserini and David Allsop",
note = "This is the author{\textquoteright}s version of a work that was accepted for publication in Nanomedicine. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Nanomedicine, 13, 2, 2017 DOI: 10.1016/j.nano.2016.10.006",
year = "2017",
month = feb,
doi = "10.1016/j.nano.2016.10.006",
language = "English",
volume = "13",
pages = "723--732",
journal = "Nanomedicine: Nanotechnology, Biology, and Medicine",
issn = "1549-9642",
publisher = "Elsevier Inc.",
number = "2",

}

RIS

TY - JOUR

T1 - Retro-inverso peptide inhibitor nanoparticles as potent inhibitors of aggregation of the Alzheimer’s Aβ peptide

AU - Gregori, Maria

AU - Taylor, Mark Neville

AU - Salvati, Elisa

AU - Re, Francesca

AU - Mancini, Simona

AU - Balducci, Claudia

AU - Forloni, Gianluigi

AU - Zambelli, Vanessa

AU - Sesana, Silvia

AU - Michael, Maria

AU - Michail, Christos

AU - Kolosov, Oleg Victor

AU - Tinker-Mill, Claire Louisa

AU - Sherer, Mike

AU - Harris, Stephen

AU - Fullwood, Nigel James

AU - Masserini, Massimo

AU - Allsop, David

N1 - This is the author’s version of a work that was accepted for publication in Nanomedicine. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Nanomedicine, 13, 2, 2017 DOI: 10.1016/j.nano.2016.10.006

PY - 2017/2

Y1 - 2017/2

N2 - Aggregation of Amyloid-β peptide (Aβ) is a key event in the pathogenesis of Alzheimer’s disease (AD). We investigated the effects of nanoliposomes decorated with the retro-inverso peptide RI-OR2-TAT (Ac-rGffvlkGrrrrqrrkkrGy-NH2) on the aggregation and toxicity of Aβ. Remarkably low concentrations of these peptide inhibitor nanoparticles (PINPs) were required to inhibit the formation of Aβ oligomers and fibrils in vitro, with 50% inhibition occurring at a molar ratio of ~1:2000 of liposome-bound RI-OR2-TAT to Aβ. PINPs also bound to Aβ with high affinity (Kd = 13.2 - 50 nM), rescued SHSY-5Y cells from the toxic effect of pre-aggregated Aβ, crossed an in vitro blood-brain-barrier model (hCMEC/D3 cell monolayer), entered the brains of C57/BL6 mice, and protected against memory loss in APPSWE transgenic mice in a novel object recognition test. As the most potent aggregation inhibitor that we have tested so far, we propose to develop PINPs as a potential disease-modifying treatment for AD.

AB - Aggregation of Amyloid-β peptide (Aβ) is a key event in the pathogenesis of Alzheimer’s disease (AD). We investigated the effects of nanoliposomes decorated with the retro-inverso peptide RI-OR2-TAT (Ac-rGffvlkGrrrrqrrkkrGy-NH2) on the aggregation and toxicity of Aβ. Remarkably low concentrations of these peptide inhibitor nanoparticles (PINPs) were required to inhibit the formation of Aβ oligomers and fibrils in vitro, with 50% inhibition occurring at a molar ratio of ~1:2000 of liposome-bound RI-OR2-TAT to Aβ. PINPs also bound to Aβ with high affinity (Kd = 13.2 - 50 nM), rescued SHSY-5Y cells from the toxic effect of pre-aggregated Aβ, crossed an in vitro blood-brain-barrier model (hCMEC/D3 cell monolayer), entered the brains of C57/BL6 mice, and protected against memory loss in APPSWE transgenic mice in a novel object recognition test. As the most potent aggregation inhibitor that we have tested so far, we propose to develop PINPs as a potential disease-modifying treatment for AD.

KW - Alzheimer’s disease

KW - liposomes

KW - retro-inverso peptide

KW - β-amyloid

KW - oligomer

U2 - 10.1016/j.nano.2016.10.006

DO - 10.1016/j.nano.2016.10.006

M3 - Journal article

VL - 13

SP - 723

EP - 732

JO - Nanomedicine: Nanotechnology, Biology, and Medicine

JF - Nanomedicine: Nanotechnology, Biology, and Medicine

SN - 1549-9642

IS - 2

ER -