Interaction with prefibrillar species and amyloid-like fibrils changes the stiffness of lipid bilayers

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

SN - 1463-9076

VL - 19

SP - 27930

EP - 27934

JO - Physical chemistry chemical physics : PCCP

JF - Physical chemistry chemical physics : PCCP

IS - 41

ER -