Research Topic

Molecular Features Linking Amyloidogenic Toxicity and Antimicrobial Peptides

About this Research Topic

Neurodegenerative, systemic, and transmissible amyloidosis are diseases where soluble proteins or peptides aggregate and deposit into β-sheet amyloid fibrils. The toxicity of amyloidotic diseases seems to be associated with the amyloid intermediate oligomeric species interaction with cell membranes, which has been suggested to several diseases, such as Alzheimer’s disease. Despite the vast amount of research and publication in this field, the molecular mechanism which turns a soluble protein or peptide into amyloid is still a matter of debate. Moreover, recent evidence suggests that amyloidogenic forms of peptides and proteins are not only toxic to its host target cells but also possess antimicrobial activity in parallel with antimicrobial peptides (AMPs). A recent hypothesis suggests an antimicrobial protective role of Aβ peptide which in certain conditions evolve to amyloid fibrils brain deposits, the hallmark of Alzheimer’s disease. Antimicrobial peptides (AMPs) are short peptides produced in a wide variety of life forms ranging from bacteria to humans having the ability to protect the host from microbial pathogens. AMPs general mechanism involves permeating membranes, facilitating membranes remodeling processes such as pore formation and fusion. The various studies on AMPs also suggest a parallel between proteins and peptides involved in amyloid diseases such as Alzheimer’s, Parkinson’s and Familial Amyloid Polyneuropathy. Notwithstanding, it has been put forward that some of the peptides involved in amyloid diseases are a conserved effector component of our innate immune system against microbial attacks and amyloid fibril formation is a result of deregulation in the control of such mechanism.

To advance our understanding and contribute to peptide design for human health and disease, it is key to comprehend the molecular features underlying amyloid precursors oligomerization and its membrane-binding properties. Besides, the characterization of the shared molecular features of amyloid diseases and antimicrobial peptides activity will be key to develop new therapeutic strategies against amyloidosis and peptide engineering for a next generation of antibiotics.

This Research Topic aims do connect two fields of biochemistry and promote the interchange of knowledge between amyloid diseases and AMPs. Areas to be covered in this Research Topic may include, but are not limited to:

• Advances in the molecular mechanism of amyloid diseases
• Molecular mechanisms of amyloidogenic intermediates toxicity
• Novel molecular features of amyloidogenic AMPs
• AMPs and amyloid protein precursors/intermediates interaction with membranes
• Functional amyloid in human health and disease
• Exploring amyloidogenicity to develop novel AMPs

Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserve the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

The Topic Editors would like to acknowledge Dr Carlos Família, who has acted as a coordinator and has contributed to the preparation of the proposal for this Research Topic.


Keywords: Amyloid protein precursors, Amyloid peptide precursors, Amyloidogenic intermediates, AMPs, the molecular mechanism of amyloid toxicity


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

Neurodegenerative, systemic, and transmissible amyloidosis are diseases where soluble proteins or peptides aggregate and deposit into β-sheet amyloid fibrils. The toxicity of amyloidotic diseases seems to be associated with the amyloid intermediate oligomeric species interaction with cell membranes, which has been suggested to several diseases, such as Alzheimer’s disease. Despite the vast amount of research and publication in this field, the molecular mechanism which turns a soluble protein or peptide into amyloid is still a matter of debate. Moreover, recent evidence suggests that amyloidogenic forms of peptides and proteins are not only toxic to its host target cells but also possess antimicrobial activity in parallel with antimicrobial peptides (AMPs). A recent hypothesis suggests an antimicrobial protective role of Aβ peptide which in certain conditions evolve to amyloid fibrils brain deposits, the hallmark of Alzheimer’s disease. Antimicrobial peptides (AMPs) are short peptides produced in a wide variety of life forms ranging from bacteria to humans having the ability to protect the host from microbial pathogens. AMPs general mechanism involves permeating membranes, facilitating membranes remodeling processes such as pore formation and fusion. The various studies on AMPs also suggest a parallel between proteins and peptides involved in amyloid diseases such as Alzheimer’s, Parkinson’s and Familial Amyloid Polyneuropathy. Notwithstanding, it has been put forward that some of the peptides involved in amyloid diseases are a conserved effector component of our innate immune system against microbial attacks and amyloid fibril formation is a result of deregulation in the control of such mechanism.

To advance our understanding and contribute to peptide design for human health and disease, it is key to comprehend the molecular features underlying amyloid precursors oligomerization and its membrane-binding properties. Besides, the characterization of the shared molecular features of amyloid diseases and antimicrobial peptides activity will be key to develop new therapeutic strategies against amyloidosis and peptide engineering for a next generation of antibiotics.

This Research Topic aims do connect two fields of biochemistry and promote the interchange of knowledge between amyloid diseases and AMPs. Areas to be covered in this Research Topic may include, but are not limited to:

• Advances in the molecular mechanism of amyloid diseases
• Molecular mechanisms of amyloidogenic intermediates toxicity
• Novel molecular features of amyloidogenic AMPs
• AMPs and amyloid protein precursors/intermediates interaction with membranes
• Functional amyloid in human health and disease
• Exploring amyloidogenicity to develop novel AMPs

Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserve the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

The Topic Editors would like to acknowledge Dr Carlos Família, who has acted as a coordinator and has contributed to the preparation of the proposal for this Research Topic.


Keywords: Amyloid protein precursors, Amyloid peptide precursors, Amyloidogenic intermediates, AMPs, the molecular mechanism of amyloid toxicity


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

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Submission Deadlines

10 January 2021 Abstract
10 May 2021 Manuscript

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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Topic Editors

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Submission Deadlines

10 January 2021 Abstract
10 May 2021 Manuscript

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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