دانلود کتاب ماده نرم بیولوژیکی

Macromolecular self-assembly is the process by which nature realizes efficient mechanisms and builds functional structures from complex tissues down to biomacromolecules. Deoxyribonucleic acids (DNAs), for instance, which through hybridization ensure the universal transmission of genetic information, are also involved in several biochemical processes such as cellular recognition mediated by cell surface receptors. Amyloids are proteinaceous fibrils that either anchor microbes to surfaces and further stabilize the bacterial biofilm or trap bacteria in a proteinaceous net in the intestine. Amyloids are functional materials but might however also be pathogenic. Amyloids have been identified in several diseases, such as neurodegenerative disorders, diabetes, and cataract. Amyloid aggregation occurs according to the nucleation polymerization of amyloidogenic peptides, being this mechanism analogous to the crystallization-driven self-assembly of synthetic polymers. Various methods and theories mastered in polymer science are currently considered to establish the mechanism of amyloid aggregation, which remains under debate, to eventually infer the pathogenic mode of structure formation and identify efficient cures against diseases for which no efficient therapeutics are available yet.