Interaction with prefibrillar species and amyloid-like fibrils changes the stiffness of lipid bilayers
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Interaction with prefibrillar species and amyloid-like fibrils changes the stiffness of lipid bilayers. / Borro, Bruno C; Parolini, Lucia; Cicuta, Pietro; Foderà, Vito; Di Michele, Lorenzo.
In: Physical chemistry chemical physics : PCCP, Vol. 19, No. 41, 25.10.2017, p. 27930-27934.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Interaction with prefibrillar species and amyloid-like fibrils changes the stiffness of lipid bilayers
AU - Borro, Bruno C
AU - Parolini, Lucia
AU - Cicuta, Pietro
AU - Foderà, Vito
AU - Di Michele, Lorenzo
PY - 2017/10/25
Y1 - 2017/10/25
N2 - Evaluating the toxicity of self-assembled protein states is a key step towards developing effective strategies against amyloidogenic pathologies such as Alzheimer's and Parkinson's diseases. Such analysis is directly connected to quantitatively probing the stability of the cellular membrane upon interaction with different protein states. Using a combination of spectroscopic techniques, morphological observations, and spectral analysis of membrane fluctuations, we identify different destabilisation routes for giant unilamellar vesicles interacting with native-like states, prefibrillar species and amyloid-like fibrils of α-lactalbumin. These effects range from substantially lowering the bending rigidity of the membranes to irreversible structural changes and complete disruption of the lipid bilayers. Our findings clearly indicate how the wide heterogeneity in structures occurring during protein aggregation can result in different destabilisation pathways, acting on different length scales and not limited to enhanced membrane permeability.
AB - Evaluating the toxicity of self-assembled protein states is a key step towards developing effective strategies against amyloidogenic pathologies such as Alzheimer's and Parkinson's diseases. Such analysis is directly connected to quantitatively probing the stability of the cellular membrane upon interaction with different protein states. Using a combination of spectroscopic techniques, morphological observations, and spectral analysis of membrane fluctuations, we identify different destabilisation routes for giant unilamellar vesicles interacting with native-like states, prefibrillar species and amyloid-like fibrils of α-lactalbumin. These effects range from substantially lowering the bending rigidity of the membranes to irreversible structural changes and complete disruption of the lipid bilayers. Our findings clearly indicate how the wide heterogeneity in structures occurring during protein aggregation can result in different destabilisation pathways, acting on different length scales and not limited to enhanced membrane permeability.
KW - Journal Article
U2 - 10.1039/c7cp05339h
DO - 10.1039/c7cp05339h
M3 - Journal article
C2 - 29028061
VL - 19
SP - 27930
EP - 27934
JO - Physical Chemistry Chemical Physics
JF - Physical Chemistry Chemical Physics
SN - 1463-9076
IS - 41
ER -
ID: 185403040