Kinetic theory of fibrillogenesis of amyloid -protein

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Kinetic theory of fibrillogenesis of amyloid beta-protein.

Prior quasielastic light scattering (QLS) studies of fibrillogenesis of synthetic amyloid beta-protein (Abeta)-(1-40) at low pH have suggested a kinetic model in which: (i) fibrillogenesis requires a nucleation step; (ii) nuclei are produced by Abeta micelles in addition to seeds initially present; and (iii) fibril elongation occurs by irreversible binding of Abeta monomers to the fibril ends. ...

متن کامل

Kinetic control of dimer structure formation in amyloid fibrillogenesis.

Amyloid fibril formation involves nonfibrillar oligomeric intermediates, which are important as possible cytotoxic species in neurodegenerative diseases. However, their transient nature and polydispersity have made it difficult to identify their formation mechanism or structure. We have investigated the dimerization process, the first step in aggregate formation, by multiple molecular dynamics ...

متن کامل

Quasielastic light scattering study of amyloid β-protein fibrillogenesis.

Quasielastic light scattering (QLS) spectroscopy is a noninvasive optical method for studying the dynamic properties of macromolecular solutions. Its most important application is the determination of diffusion coefficients, from which the sizes of particles in solution may be estimated. The technique thus is particularly useful for monitoring assembly (polymerization and aggregation) reactions...

متن کامل

Kinetic theory of amyloid fibril templating.

The growth of amyloid fibrils requires a disordered or partially unfolded protein to bind to the fibril and adapt the same conformation and alignment established by the fibril template. Since the H-bonds stabilizing the fibril are interchangeable, it is inevitable that H-bonds form between incorrect pairs of amino acids which are either incorporated into the fibril as defects or must be broken ...

متن کامل

Brazilin inhibits amyloid β-protein fibrillogenesis, remodels amyloid fibrils and reduces amyloid cytotoxicity

Soluble amyloid β-protein (Aβ) oligomers, the main neurotoxic species, are predominantly formed from monomers through a fibril-catalyzed secondary nucleation. Herein, we virtually screened an in-house library of natural compounds and discovered brazilin as a dual functional compound in both Aβ42 fibrillogenesis inhibition and mature fibril remodeling, leading to significant reduction in Aβ42 cy...

متن کامل

ذخیره 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: Proceedings of the National Academy of Sciences

سال: 1997

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.94.15.7942