Binding of Aβ peptide creates lipid density depression in DMPC bilayer
نویسندگان
چکیده
منابع مشابه
Structure of the DMPC lipid bilayer ripple phase.
High resolution structure is presented for the ripple (Pβ') phase of the phospholipid dimyristoylphosphatidylcholine. Low angle X-ray scattering from oriented samples yielded 57 orders, more than twice as many as recorded previously. The determined electron density map has a sawtooth profile similar to the result from lower resolution data, but the features are sharper allowing better estimates...
متن کاملModification of the CHARMM force field for DMPC lipid bilayer
The CHARMM force field for DMPC lipids was modified in order to improve agreement with experiment for a number of important properties of hydrated lipid bilayer. The modification consists in introduction of a scaling factor 0.83 for 1-4 electrostatic interactions (between atoms separated by three covalent bonds), which provides correct transgauche ratio in the alkane tails, and recalculation of...
متن کاملDiffusion of water and selected atoms in DMPC lipid bilayer membranes.
Molecular dynamics simulations have been used to determine the diffusion of water molecules as a function of their position in a fully hydrated freestanding 1,2-dimyristoyl-sn-glycero-3-phosphorylcholine (DMPC) bilayer membrane at 303 K and 1 atm. The diffusion rate of water in a ∼10 Å thick layer just outside the membrane surface is reduced on average by a factor of ∼2 relative to bulk. For wa...
متن کاملAlzheimer Aβ peptide interactions with lipid membranes
Fibrillar aggregates of misfolded amyloid proteins are involved in a variety of diseases such as Alzheimer disease (AD), type 2 diabetes, Parkinson, Huntington and prion-related diseases. In the case of AD amyloid β (Aβ) peptides, the toxicity of amyloid oligomers and larger fibrillar aggregates is related to perturbing the biological function of the adjacent cellular membrane. We used atomisti...
متن کاملThermodynamics of Peptide Insertion and Aggregation in a Lipid Bilayer
A variety of biomolecules mediate physiological processes by inserting and reorganizing in cell membranes, and the thermodynamic forces responsible for their partitioning are of great interest. Recent experiments provided valuable data on the free energy changes associated with the transfer of individual amino acids from water to membrane. However, a complete picture of the pathways and the ass...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 2014
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2014.07.010