By Ehud Gazit
Written by way of a number one nanobiologist actively concerned on the vanguard of the sphere either as a researcher and an educator, this booklet takes the reader from the basics of nanobiology to the main complex functions.
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Extra resources for Plenty of Room for Biology at the Bottom: An Introduction to Bionanotechnology
Yet, it plays a central medical role as well as an emerging role in the field of nanobiotechnology. Amyloid assemblies are nano-scale fibrils that are characteristic of a large group of diseases of unrelated origin. A partial list of amyloidassociated diseases includes Alzheimer’s disease, Type II diabetes, primary and secondary amyloidosis, and Prion diseases (such as BSE – Bovine Spongiform Encephalopathy, also known as the “the mad-cow disease”). , in the brains of Alzheimer’s disease patients or in the pancreas of Type II diabetes patients).
The driving force for the formation of the assemblies is the amphiphatic nature of the phospholipids building blocks. The phospholipids building block is an amphiphilic molecule that has a hydrophilic part, the phosphate head group, and a hydrophobic, an aliphatic tail. Upon transfer of phospholipids molecules into aqueous solution a rapid and spontaneous association of the molecules occur during the enormous energetic cost of the presence of the aliphatic tail in water. The organization of the phospholipids is into bilayres structure in which each of the aliphatic parts of each layer are pointed towards each Natural Biological Assembly at the Nano-Scale 41 other and the hydrophilic heads are pointed either to the bulk water or to the inside part of the closed structure.
2003) as will be further illustrated in Chapter 6. The recognition principles as implicated in the formation of amyloid fibrils and most notably the key use of aromatic interactions were later used in the design and fabrication of nanotubes and nanospheres. 9. Silk: Natural Fibrillar Supramolecular Protein Assembly The natural fibrillar supramolecular structures that are mostly related to amyloid fibrils, as discussed above, are those of spider and worm silk. These fibrils are predominantly composed of two protein molecules that create macroscopic filaments by precise molecular recognition and selfassembly process (Kubic, 2002; Jin and Kaplan, 2003).