Protein conversion from a water-soluble native conformation to the insoluble aggregates and fibrils, which can deposit in amyloid ...
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Protein conversion from a water-soluble native conformation to the insoluble aggregates and fibrils, which can deposit in amyloid plaques, underlies more than 20 human diseases, representing a major public health problem and a scientific challenge. Such a conversion is called protein misfolding. Protein misfolding can also involve errors in the topology of the folded proteins and their assembly in lipid membranes. Lipids are found in nearly all amyloid deposits in vivo, and can critically influence protein misfolding in vitro and in vivo in many different ways. This book focuses on recent advances in our understanding of the role of lipids in modulating the misfolding of various proteins. The main emphasis is on the basic biophysical studies that address molecular basis of protein misfolding and amyloid formation, and the role of lipids in this complex process.
Explains how protein misfolding is an important biological phenomenon underlying over 20 major human diseases Shows that Lipids importantly influence protein misfolding and amyloid diseases Provides an up-to-date analysis of the roles of lipids in protein misfolding Discusses a wide array of proteins, lipids and their modes of interaction Focusses on the biophysical and structural properties of the interacting partners Complements the small collection of books on this topic in this rapidly developing field Klappentext This book addresses molecular mechanisms of protein misfolding and the role of lipids and related molecules in these complex processes. The focus is on the biophysical and structural studies of proteins that are involved in major human disorders such as Alzheimer's disease, systemic amyloidoses, diabetes II, inflammation and atherosclerosis. Misfolding often results from protein mutations or modifications. Misfolding of membrane proteins can cause topological changes that target the proteins for degradation. Misfolding of soluble globular proteins and peptides converts them into -sheet-rich aggregates and amyloid fibrils. This process can disrupt the structural integrity of the lipid membranes and thereby contribute to amyloid toxicity. In turn, lipids and lipid-associated molecules such as apolipoproteins and heparan sulfate proteoglycans, which are ubiquitous constituents of amyloid plaques, can influence protein misfolding via diverse mechanisms that are addressed in this book. The book features chapters describing the role of lipids in the misfolding of a wide range of proteins, including small peptides, globular proteins, lipid surface-binding proteins, and integral membrane proteins. The role of individual lipid molecules, lipid surfaces, and the membrane field is addressed, including specific and non-specific interactions with protein oligomers and mature fibrils. Distinct effects of various lipids on the nucleation and growth of amyloid fibrils are discussed. Modern computational approaches to the analysis of amyloid formation are addressed. The book should be useful to experts in the field but is also accessible to novices. Inhalt 1. Role of Lipids in Folding, Misfolding and Function of Integral Membrane Proteins; Heedeok Hong2. Protein Misfolding in Lipid-Mimetic Environments; Vladimir N. Uversky 3. Lipids in Amyloid- Processing, Aggregation, and Toxicity; Isabel Morgado and Megan Garvey4. Role of Cholesterol and Phospholipids in Amylin Misfolding, Aggregation and Etiology of Islet Amyloidosis; Sanghamitra Singh, Saurabh Trikha, Diti Chatterjee Bhowmick, Anjali A. Sarkar and Aleksandar M. Jeremic5. Stability, Oligomerization, and Amyloidogenicity of Apo Serum Amyloid A; Wilfredo Colón, J. Javier Aguilera, and Saipraveen Srinivasan6. Interactions of Lipid Membranes with Fibrillar Protein Aggregates; Galyna Gorbenko, Valeriya Trusova, Mykhailo Girych, Emi Adachi, Chiharu Mizuguchi, and Hiroyuki Saito7. The Role of Lipid in Misfolding and Amyloid Fibril Formation by Apolipoprotein C-II; Timothy M. Ryan, Yee-Foong Mok , Geoffrey J. Howlett and Michael D.W. Griffin8. Amyloid-Forming Properties of Human Apolipoproteins: Sequence Analyses and Structural Insights; Madhurima Das and Olga Gursky9. Computational Approaches to Identification of Aggregation Sites and the Mechanism of Amyloid Growth; Nikita V. Dovidchenko and Oxana V. Galzitskaya10. Role of Syndecans in Lipid Metabolism and Human Diseases; Elena I. Leonova and Oxana V. Galzitskaya