Amyloid fibril formation is suppressed in microgravity
نویسندگان
چکیده
منابع مشابه
Collagen Fibril Formation at Microgravity Conditions:
Collagen molecules can selfassemble from dilute solutions into axially ordered fibrils similar to those seen in vivo in tendon and skin. At neutral pH the self-assembly has a negative temperature coefficient, thus molecules can be held in solution at 4-15 C; a temperature jump to 25-30 C will then lead to fibrillogenesis under controlled conditions. Two experiments have been carried out under...
متن کاملSurface-catalyzed amyloid fibril formation.
Light chain (or AL) amyloidosis is characterized by the pathological deposition of insoluble fibrils of immunoglobulin light chain fragments in various tissues, walls of blood vessels, and basement membranes. In the present investigation, the in vitro assembly of a recombinant amyloidogenic light chain variable domain, SMA, on various surfaces was monitored using atomic force microscopy. SMA fo...
متن کاملButyrylcholinesterase attenuates amyloid fibril formation in vitro.
In Alzheimer's disease, both acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) colocalize with brain fibrils of amyloid-beta (Abeta) peptides, and synaptic AChE-S facilitates fibril formation by association with insoluble Abeta fibrils. Here, we report that human BChE and BSP41, a synthetic peptide derived from the BChE C terminus, inversely associate with the soluble Abeta conformer...
متن کاملEffect of Surfaces on Amyloid Fibril Formation
Using atomic force microscopy (AFM) we investigated the interaction of amyloid beta (Aβ) peptide with chemically modified surfaces in order to better understand the mechanism of amyloid toxicity, which involves interaction of amyloid with cell membrane surfaces. We compared the structure and density of Aβ fibrils on positively and negatively charged as well as hydrophobic chemically-modified su...
متن کاملPathways and intermediates of amyloid fibril formation.
The lack of understanding of amyloid fibril formation at the molecular level is a major obstacle in devising strategies to interfere with the pathologies linked to peptide or protein aggregation. In particular, little is known on the role of intermediates and fibril elongation pathways as well as their dependence on the intrinsic tendency of a polypeptide chain to self-assembly by beta-sheet fo...
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: Biochemistry and Biophysics Reports
سال: 2021
ISSN: 2405-5808
DOI: 10.1016/j.bbrep.2020.100875