Dear Colleagues,

Alpha-synuclein is acknowledged for its potential role in a range of diseases, termed synucleinopathies. The most well-known of these diseases is Parkinson’s disease. In these diseases, alpha-synuclein is mostly identified as an aggregated protein frequently found in deposits, such as Lewy Bodies. Like many proteins associated with neurodegenerative disease, the aggregated protein is an abnormal form of a protein expressed in healthy neurons. Recent research has produced a range of interesting insights into the function and behaviour of alpha-synuclein. While, the protein has long been considered a largely unfolded monomer, there is now evidence that the functional form is a helical tetramer. Similarly, more information on molecular functions have come to light which include a potential role in dopamine transport, and a possible enzymatic role as a ferrireductase, increasing the levels of ferrous iron in the cell.

Similarly, the study of the aggregated form of alpha-synuclein used to focus on the formation of fibrils. However, there has been greater emphasis on the ability of alpha-synuclein to form oligomeric species that can induced pathological changes. Such changes include indirect effects, such as altered microglial activation or direct effects, such as toxicity to neurons possibly mediated through molecules, such as FoxO3a. These different finding imply that the polymerisation state of alpha-synuclein (tetramer or oligomer) may direct its fate within the cell and impact downstream the viability of dopaminergic neurons. Finally, the potential role of the homologue, beta-synuclein has emerged as a possible counter to the negative effects of alpha-synuclein. Beta-synuclein is transcriptionally coupled to alpha-synuclein and it can physically impede alpha-synuclein aggregation.

Given these new insight into the function and dysfunction of alpha-synuclein this special edition of Biomolecules is very timely. This provides an opportunity for recent work in these areas to be presented in unison along with critical reviews of such recent work. Submission of studies of molecular aspects of synuclein activity are therefore greatly encourage.

Prof. David R. Brown
Guest Editor

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• Alpha-synuclein
• Beta-synuclein
• Neurodegeneration
• Protein aggregation
• Synucleinopathies
• Dopamine synthesis, transport and metabolism
• Tetramer formation
• Parkinson’s Disease
• Structure-function relation in proteins
• Age-related disease
• Molecular modelling of proteins Rational design for drug targeting