ABSTRACT
At least 30,000 different proteins are produced by human cells, and each has a different role. Each protein is characterized by its own unique sequence and native conformation in order to perform its specic function. Hence, an altered folding, cleavage, or amino acid sequence of proteins may lead to serious disorders. Protein misfolding often leads to protein aggregation and precipitation, with the aggregates adopting either highly ordered (amyloid bril) or disordered (amorphous) forms leading to disease. For instance, amyloid brils are connected to a variety of debilitating diseases, including Alzheimer’s, Parkinson’s, Huntington’s, and Creutzfeldt-Jakob’s diseases, as well as type 2 diabetes. There is more and more information available showing the interrelationship between genomic instability and diseases such as cancer initiation and progression, where numerous genomic lesions (point mutations, deletions, and insertions) lead to expression of proteins with altered sequences and properties. In order to be able to ght these devastating disorders, huge research efforts are today devoted to understand the molecular mechanisms behind the disorders. In Part V, Chapters 28-31, the introduction to diseases related to misfolding, miscleavage, and mis-sequences of proteins is presented, together with summary of recent achievements in available applications and future possibilities of using peptides and proteins as drugs.
