Helix-A peptide prevents gp120-mediated neuronal loss

Research output: Contribution to journalArticle

Valeria Avdoshina, Francesca Taraballi, Ennio Tasciotti, Aykut Üren, Italo Mocchetti

Aim: The human-immunodeficiency virus (HIV) envelope protein gp120 promotes synaptic damage similar to that observed in people living with HIV who have neurocognitive disorders. The neurotoxic effect of gp120 appears to occur through the α-helix motif that binds to neuronal microtubules (MTs). In this study, we examined the ability of short peptide derivatives from Helix-A, a peptide synthesized based on α-helix structure of gp120, to displace gp120 from binding to MTs and prevent its neurotoxic effects. Methods: Surface plasmon resonance was used to determine the binding of Helix-A and its modifications to MTs. Helix-A peptide and derivatives were delivered inside rat primary cortical neurons by mesoporous silica nanoparticles (MSN). Neuronal processes and survival were evaluated by microtubule associated protein 2-immunostaining and Hoechst/Propidium iodide, respectively. Results: Surface plasmon resonance analysis revealed that Helix-A but not its modifications binds to MTs. Also, only Helix-A MSN but not other peptides prevented the ability of gp120 to reduce neuronal processes as well as neuronal survival. Thus, the amino acid structure of Helix-A is key for its neuroprotective activity.

Original languageEnglish (US)
Article number61
JournalMolecular Brain
Volume12
Issue number1
DOIs
StatePublished - Jun 25 2019

PMID: 31238994

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Helix-A peptide prevents gp120-mediated neuronal loss. / Avdoshina, Valeria; Taraballi, Francesca; Tasciotti, Ennio; Üren, Aykut; Mocchetti, Italo.

In: Molecular Brain, Vol. 12, No. 1, 61, 25.06.2019.

Research output: Contribution to journalArticle

Harvard

Avdoshina, V, Taraballi, F, Tasciotti, E, Üren, A & Mocchetti, I 2019, 'Helix-A peptide prevents gp120-mediated neuronal loss' Molecular Brain, vol. 12, no. 1, 61. https://doi.org/10.1186/s13041-019-0482-z

APA

Avdoshina, V., Taraballi, F., Tasciotti, E., Üren, A., & Mocchetti, I. (2019). Helix-A peptide prevents gp120-mediated neuronal loss. Molecular Brain, 12(1), [61]. https://doi.org/10.1186/s13041-019-0482-z

Vancouver

Avdoshina V, Taraballi F, Tasciotti E, Üren A, Mocchetti I. Helix-A peptide prevents gp120-mediated neuronal loss. Molecular Brain. 2019 Jun 25;12(1). 61. https://doi.org/10.1186/s13041-019-0482-z

Author

Avdoshina, Valeria ; Taraballi, Francesca ; Tasciotti, Ennio ; Üren, Aykut ; Mocchetti, Italo. / Helix-A peptide prevents gp120-mediated neuronal loss. In: Molecular Brain. 2019 ; Vol. 12, No. 1.

BibTeX

@article{a6daff03d94647b3aca0900b7bc36491,
title = "Helix-A peptide prevents gp120-mediated neuronal loss",
abstract = "Aim: The human-immunodeficiency virus (HIV) envelope protein gp120 promotes synaptic damage similar to that observed in people living with HIV who have neurocognitive disorders. The neurotoxic effect of gp120 appears to occur through the α-helix motif that binds to neuronal microtubules (MTs). In this study, we examined the ability of short peptide derivatives from Helix-A, a peptide synthesized based on α-helix structure of gp120, to displace gp120 from binding to MTs and prevent its neurotoxic effects. Methods: Surface plasmon resonance was used to determine the binding of Helix-A and its modifications to MTs. Helix-A peptide and derivatives were delivered inside rat primary cortical neurons by mesoporous silica nanoparticles (MSN). Neuronal processes and survival were evaluated by microtubule associated protein 2-immunostaining and Hoechst/Propidium iodide, respectively. Results: Surface plasmon resonance analysis revealed that Helix-A but not its modifications binds to MTs. Also, only Helix-A MSN but not other peptides prevented the ability of gp120 to reduce neuronal processes as well as neuronal survival. Thus, the amino acid structure of Helix-A is key for its neuroprotective activity.",
keywords = "Dendritic simplification, HAND, HIV, Mesoporous nanoparticles, Microtubules, Neuronal survival",
author = "Valeria Avdoshina and Francesca Taraballi and Ennio Tasciotti and Aykut {\"U}ren and Italo Mocchetti",
year = "2019",
month = "6",
day = "25",
doi = "10.1186/s13041-019-0482-z",
language = "English (US)",
volume = "12",
journal = "Molecular brain",
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publisher = "BioMed Central Ltd.",
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RIS

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T1 - Helix-A peptide prevents gp120-mediated neuronal loss

AU - Avdoshina, Valeria

AU - Taraballi, Francesca

AU - Tasciotti, Ennio

AU - Üren, Aykut

AU - Mocchetti, Italo

PY - 2019/6/25

Y1 - 2019/6/25

N2 - Aim: The human-immunodeficiency virus (HIV) envelope protein gp120 promotes synaptic damage similar to that observed in people living with HIV who have neurocognitive disorders. The neurotoxic effect of gp120 appears to occur through the α-helix motif that binds to neuronal microtubules (MTs). In this study, we examined the ability of short peptide derivatives from Helix-A, a peptide synthesized based on α-helix structure of gp120, to displace gp120 from binding to MTs and prevent its neurotoxic effects. Methods: Surface plasmon resonance was used to determine the binding of Helix-A and its modifications to MTs. Helix-A peptide and derivatives were delivered inside rat primary cortical neurons by mesoporous silica nanoparticles (MSN). Neuronal processes and survival were evaluated by microtubule associated protein 2-immunostaining and Hoechst/Propidium iodide, respectively. Results: Surface plasmon resonance analysis revealed that Helix-A but not its modifications binds to MTs. Also, only Helix-A MSN but not other peptides prevented the ability of gp120 to reduce neuronal processes as well as neuronal survival. Thus, the amino acid structure of Helix-A is key for its neuroprotective activity.

AB - Aim: The human-immunodeficiency virus (HIV) envelope protein gp120 promotes synaptic damage similar to that observed in people living with HIV who have neurocognitive disorders. The neurotoxic effect of gp120 appears to occur through the α-helix motif that binds to neuronal microtubules (MTs). In this study, we examined the ability of short peptide derivatives from Helix-A, a peptide synthesized based on α-helix structure of gp120, to displace gp120 from binding to MTs and prevent its neurotoxic effects. Methods: Surface plasmon resonance was used to determine the binding of Helix-A and its modifications to MTs. Helix-A peptide and derivatives were delivered inside rat primary cortical neurons by mesoporous silica nanoparticles (MSN). Neuronal processes and survival were evaluated by microtubule associated protein 2-immunostaining and Hoechst/Propidium iodide, respectively. Results: Surface plasmon resonance analysis revealed that Helix-A but not its modifications binds to MTs. Also, only Helix-A MSN but not other peptides prevented the ability of gp120 to reduce neuronal processes as well as neuronal survival. Thus, the amino acid structure of Helix-A is key for its neuroprotective activity.

KW - Dendritic simplification

KW - HAND

KW - HIV

KW - Mesoporous nanoparticles

KW - Microtubules

KW - Neuronal survival

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