Molecular Mechanisms of Turnover and Toxicity of Amyloid Proteins From Cells to Treatments

A special issue of Chemistry (ISSN 2624-8549). This special issue belongs to the section "Medicinal Chemistry".

Deadline for manuscript submissions: closed (31 August 2021) | Viewed by 258

Special Issue Editor

Department of Biological Sciences, The George Washington University, Washington, DC, USA
Interests: islet biology; amyloidosis; β-cell function; protein trafficking and proteotoxicity
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Amyloidosis is a biological event in which proteins undergo structural/physical transitions from soluble monomers and oligomers to insoluble beta-sheet enriched fibrillar aggregates. Exactly how and why amyloid proteins aggregate is still not well understood. This Special Issue brings together biochemistry, biophysics, structural/cell biology, and medicine to discuss cutting-edge research on molecular mechanisms and the novel treatments of a broad range of amyloid diseases. We summarize the main mechanisms of (mis)folding, trafficking, and toxicity of amyloid proteins and peptides in eukaryotic cells.

We also discuss how a structurally and functionally diverse class of amyloid proteins are recognized and degraded by cells and describe cellular and therapeutic strategies to evade or halt toxic structural protein forms. In addition to exploring the fundamental question of how cells distinguish between toxic and non-toxic amyloid species, we also discuss the mechanisms of amylin transport across the cell plasma membrane and their intracellular trafficking and recycling pathways. This issue also examines amylin folding intermediates and defines the role of membrane cholesterol and lipids in amyloid protein’s structural conversions; it unravels amino acids and lipids driving amylin’s structural transitions in solution and on membranes; it investigates internalization, trafficking, and secretory pathways of amyloid proteins and uncovers the roles of amyloid receptors and other signaling molecules in amyloid-induced cellular stress. Finally, the role of various proteolytic systems and amyloid modulators, synthetic and natural, in turnover and toxicity of amyloid proteins is illuminated.

With the aid of biophysical, biochemical, molecular imaging, and genetic approaches, a diverse group of scientists deliberate in this Special Issue the molecular and biochemical events leading to the formation of amyloid oligomers and aggregates or plaques. This knowledge is critical for the development of novel therapeutics for the treatment of metabolic, neurological, and other amyloid-associated disorders.

You may choose our Joint Special Issue in Molecules.

Dr. Aleksandar M. Jeremic
Guest Editor

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Keywords

  • Structure and function of amyloid proteins
  • Protein oligomerization and aggregation pathways in vitro and in vivo
  • Trafficking, secretory, and recycling pathways of amyloid proteins
  • Amyloid receptors and cell signaling
  • Proteotoxicity
  • Proteasome and proteolytic enzymes in amyloid clearance
  • Autophagy and amyloid formation
  • Small molecules and natural amyloid inhibitors
  • Amyloid pathology and drug design
  • Computational tools/bioinformatics in understanding amyloidosis

Related Special Issue

Published Papers

There is no accepted submissions to this special issue at this moment.
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