Structural model of Alzheimer Amyloid A-beta 1 - 42
peptide fibril derived from an experimental structure (PDB: 2MXU).
This A-beta
peptide fibril has been rendered in 3 - D by a transmission electron microscope, providing the most detailed look yet at the telltale sign of Alzheimer's disease.
It has been demonstrated that silk properties (in terms of different reeling methods [32], [42], environmental conditions [8], [20], types of silk [e.g. dragline, viscid or egg sac silk][22], [24], [34]-RRB- are species - specific and lead to silk - based
peptide fibrils or protein aggregates with different structural and mechanical properties.
Not exact matches
The platform builds the
fibrils by combining the properties of the nanotube with a synthetic
peptide fragment that is placed inside the cylinder.
This
peptide, 39 to 42 amino acids long, is toxic to nerve cells and is able to form elongated
fibrils.
A European research team and a team from the United States (Massachussetts Institute of Technology in cooperation with Lund University) have simultaneously succeeded in elucidating the structure of the most disease - relevant beta - amyloid
peptide 1 - 42
fibrils at atomic resolution.
Many
peptides and proteins have an innate ability to assemble into long, slender fibers called
fibrils and other shapes.
Four of the mAbs, 2T5C9, 2G9C, T1F11, and TB2H7, demonstrated diagnostic potential in enzyme - linked immunosorbent assays (ELISA) by their low to sub-nanomolar cross-reactivity with recombinant wild - type (WT) and mutant TTR aggregates and lack of binding to native TTR or amyloid
fibrils formed by other
peptides or proteins.
This toxicity is mediated by the fibrillar form of the amylin
peptide and requires direct contact of the
fibrils with the cell surface.