Amyloid refers to the abnormal fibrous, extracellular, proteinaceous deposits found in

organs and tissues. Amyloid is insoluble and is structurally dominated by β-sheet

structure. Unlike other fibrous proteins it does not commonly have a structural,
supportive or motility role but is associated with the pathology seen in a range of
diseases known as the amyloidoses. These diseases include Alzheimer's, the spongiform
encephalopathies and type II diabetes, all of which are progressive disorders with
associated high morbidity and mortality. Not surprisingly, research into the
physicochemical properties of amyloid and its formation is currently intensely pursued.
In this chapter we will highlight the key scientific findings and discuss how the stability
of amyloid fibrils impacts on bionanotechnology.

The name amyloid comes from the early mistaken identification by Rudolf virchow of
the substance as starch, based on crude iodine-staining techniques.
Non desease and functional amyloids
Many examples of non-pathological amyloid with a well-defined physiological role
have been identified in various organisms, including human. These may be termed as
functional or physiological orn ative amyloid
Functional amyloid in Homo sapiens
Intralumental domain of melanocyte protein PMEL.
Peptide/protein hormones stored as amyloids within endocrine secretory granules.
Receptor-interaction serine/threonine-protein kinase
Fragments of prostatic acid and phosphatase and semenogelins
Functional amyloid in Other organisms
Curli fibrils produced by E.coli, salmonella, and a few Other membrans of the
enterobacteriales, The genetic elements encoding the curli system are phylogenic
widespread and can be found in at least four bacterial phyla.

What is amyloid fibrils?

Amyloid fibrils are elongated protein aggregates well known for their association with many
human diseases. However, similar structures have also been found in other organisms and
amyloid fibrils can also be formed in vitro by other proteins usually under non-physiological
conditions. In all cases, these fibrils assemble in a nucleated polymerization reaction with a
pronounced lag phase that can be eliminated by supplying pre-formed fibrils as seeds.

How structure amyloid fibrils?

Amyloids are formed of long unbranched fibers that are characterized by an extended beta-
sheet secondary structure in which individual beta strands (β-strands) (coloured arrows in
the adjacent figure) are arranged in an orientation perpendicular to the long axis of the
fiber. Such a structure is known as cross-β structure.

Amyloid fibrils are regular, β-sheet-enriched, long, nanoscale aggregates of proteins with b-strands
running perpendicular to the long axis of the fibril. Amyloid fibrils were first found in the tissue of patients
suffering from neurodegenerative diseases. Amyloidosis is a great problem of medicine because a number
of human diseases (including Alzheimer’s disease, Parkinson’s disease, transmissible
spongiform encephalopathies, dialysis amyloidosis, etc.) are characterized by intracellular inclusions or
extracellular deposits of proteins in the form of amyloid fibrils.
It is now clear that amyloid fibrils concern many other aspects. The formation of amyloid-like fibrils
frequently accompanies over-expression of the recombinant proteins, thus hampering the technology
process. However, due to unique architectures and exceptional properties (e.g., high mechanical strength),
amyloid fibrils appeared an attractive subject in materials science and nanobiotechnology. Furthermore,
the investigations of the structure of amyloid fibrils and the molecular mechanisms of their formation are
important for the basic problem of protein folding, because it was found that not only proteins associated
with the diseases, but practically all (or most) proteins are prone to form amyloid fibrils in appropriate
conditions. Consequently, the ability to fibrillate is a generic property of a polypeptide chain, and the
amyloid fibril is a unique state of proteins. However, the formation of amyloid fibrils is most likely by
intrinsically disordered proteins (IDPs), because their disordered regions which are important for the ability
to interact with their partners are also responsible for a great danger of their aggregation and the formation
of amyloid fibrils.

The adjacente figure are arranged in na orientation

Function amyloid fibrils?

Role amyloid fibrils Other than desease?

Mechanisme amyoid fibrils?

Process amyloid fibrils?

Conclution?