TY - JOUR
T1 - Hydrophobic-Interaction-Induced Stiffening of α-Synuclein Fibril Networks
AU - Semerdzhiev, Slav A.
AU - Lindhoud, Saskia
AU - Stefanovic, Anja
AU - Subramaniam, Vinod
AU - van der Schoot, Paul
AU - Claessens, Mireille M.A.E.
PY - 2018/5/17
Y1 - 2018/5/17
N2 - In water, networks of semiflexible fibrils of the protein α-synuclein stiffen significantly with increasing temperature. We make plausible that this reversible stiffening is a result of hydrophobic contacts between the fibrils that become more prominent with increasing temperature. The good agreement of our experimentally observed temperature dependence of the storage modulus of the network with a scaling theory linking network elasticity with reversible cross-linking enables us to quantify the endothermic binding enthalpy and estimate the effective size of hydrophobic patches on the fibril surface. Our findings may not only shed light on the role of amyloid deposits in disease conditions, but can also inspire new approaches for the design of thermoresponsive materials.
AB - In water, networks of semiflexible fibrils of the protein α-synuclein stiffen significantly with increasing temperature. We make plausible that this reversible stiffening is a result of hydrophobic contacts between the fibrils that become more prominent with increasing temperature. The good agreement of our experimentally observed temperature dependence of the storage modulus of the network with a scaling theory linking network elasticity with reversible cross-linking enables us to quantify the endothermic binding enthalpy and estimate the effective size of hydrophobic patches on the fibril surface. Our findings may not only shed light on the role of amyloid deposits in disease conditions, but can also inspire new approaches for the design of thermoresponsive materials.
UR - http://www.scopus.com/inward/record.url?scp=85047181721&partnerID=8YFLogxK
U2 - 10.1103/PhysRevLett.120.208102
DO - 10.1103/PhysRevLett.120.208102
M3 - Article
C2 - 29864360
AN - SCOPUS:85047181721
SN - 0031-9007
VL - 120
JO - Physical review letters
JF - Physical review letters
IS - 20
M1 - 208102
ER -