The amyloid interactome: Exploring protein aggregation

Protein-protein interactions are the quintessence of physiological activities, but also participate in pathological conditions. Amyloid formation, an abnormal protein-protein interaction process, is a widespread phenomenon in divergent proteins and peptides, resulting in a variety of aggregation dis...

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Bibliographic Details
Published in:	PloS one 2017-03, Vol.12 (3), p.e0173163-e0173163
Main Authors:	Biza, Konstantina V, Nastou, Katerina C, Tsiolaki, Paraskevi L, Mastrokalou, Chara V, Hamodrakas, Stavros J, Iconomidou, Vassiliki A
Format:	Article
Language:	eng
Subjects:	Agglomeration Alzheimers disease Amyloid Amyloid - chemistry Amyloid - metabolism Amyloid beta-protein Amyloidogenesis Amyloidosis - metabolism Analysis Biology Biology and Life Sciences Biophysics Computer and Information Sciences Computer applications Disorders Experiments Heat shock proteins Humans Molecular structure Neurobiology Neurosciences Peptides Protein Aggregation, Pathological - metabolism Protein folding Protein interaction Protein Interaction Maps Protein-protein interactions Proteins Quintessence (cosmology) Self assembly Studies
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Summary:	Protein-protein interactions are the quintessence of physiological activities, but also participate in pathological conditions. Amyloid formation, an abnormal protein-protein interaction process, is a widespread phenomenon in divergent proteins and peptides, resulting in a variety of aggregation disorders. The complexity of the mechanisms underlying amyloid formation/amyloidogenicity is a matter of great scientific interest, since their revelation will provide important insight on principles governing protein misfolding, self-assembly and aggregation. The implication of more than one protein in the progression of different aggregation disorders, together with the cited synergistic occurrence between amyloidogenic proteins, highlights the necessity for a more universal approach, during the study of these proteins. In an attempt to address this pivotal need we constructed and analyzed the human amyloid interactome, a protein-protein interaction network of amyloidogenic proteins and their experimentally verified interactors. This network assembled known interconnections between well-characterized amyloidogenic proteins and proteins related to amyloid fibril formation. The consecutive extended computational analysis revealed significant topological characteristics and unraveled the functional roles of all constituent elements. This study introduces a detailed protein map of amyloidogenicity that will aid immensely towards separate intervention strategies, specifically targeting sub-networks of significant nodes, in an attempt to design possible novel therapeutics for aggregation disorders.
ISSN:	1932-6203 1932-6203