Special Issue "Protein Aggregation"
Deadline for manuscript submissions: closed (30 November 2011)
Prof. Dr. Ludmilla A. Morozova-Roche (Website)
Department of Medical Biochemistry and Biophysics, Umeå University, Umeå, SE 90781, Sweden
Phone: +46 90 786 5283
Fax: +46 90 786 9795
Interests: amyloid; protein folding; neurodegeneration; inflammation; amyloid diseases
Protein aggregation is the most common and problematic manifestation of protein instability encountered during all stages of protein purification and applications. The formation of unstructured aggregates effectively reduces the quantity of functional compounds in solutions. If protein aggregates are not eliminated by clearance mechanisms from the body, the accumulation of protein deposits is associated with growing number of protein conformational diseases. Among proteins aggregates the structured aggregation involving the formation of cross-beta-sheet containing amyloid fibrils and oligomers received particular attention being a leading course of age-related degenerative amyloid diseases. Evidence accumulated that in some cases the regulated protein aggregation can fulfill useful functions of polypeptide storage or sequestration and minimization of diffusion of highly reactive and toxic species. As a result the protein aggregation became the central theme of much current research aimed at understanding the mechanisms underlying this process and measures increasing proteins stability and reducing the propensity of the spontaneous and often undesirable aggregation. Here we present the collection of articles presenting the broad overview of the state of this rapidly developing field and the challenges met by using current knowledge of the mechanisms of protein molecular assemblies and stability.
Prof. Dr. Ludmilla A. Morozova-Roche
- protein aggregation
- amyloid formation
- conformational plasticity