Natural Antimicrobial Peptides Self-assemble as α/β Chameleon Amyloids Article Swipe
Peleg Ragonis‐Bachar
,
Bader Rayan
,
Eilon Barnea
,
Yizhaq Engelberg
,
Alexander Upcher
,
Meytal Landau
·
YOU?
·
· 2022
· Open Access
·
· DOI: https://doi.org/10.1101/2022.06.23.497336
YOU?
·
· 2022
· Open Access
·
· DOI: https://doi.org/10.1101/2022.06.23.497336
Amyloid protein fibrils and some antimicrobial peptides (AMPs) share biophysical and structural properties. This observation suggests that ordered self-assembly can act as an AMP-regulating mechanism, and, vice versa, that human amyloids play a role in host defense against pathogens, as opposed to their common association with neurodegenerative and systemic diseases. Based on previous structural information on toxic amyloid peptides, we developed a sequence-based bioinformatics platform and, led by its predictions, experimentally identified 14 fibril-forming AMPs (ffAMPs) from living organisms, which demonstrated cross-β and cross-α amyloid properties. The results support the amyloid-antimicrobial link. The high prevalence of ffAMPs produced by amphibians and marine creatures among other species suggests that they confer unique advantageous properties in distinctive environments, potentially providing stability and adherence properties. Most of the newly identified 14 ffAMPs showed lipid-induced and/or time-dependent secondary structure transitions in the fibril form, indicating structural and functional cross-α/β chameleons. Specifically, ffAMP cytotoxicity against human cells correlated with inherent or lipid-induced α-helical fibril structure. The findings raise hypotheses about the role of fibril secondary structure switching in regulation of processes, such as the transition between a stable storage conformation and an active state with toxicity against specific cell types.
Related Topics
Concepts
Fibril
Creatures
Amyloid (mycology)
Amyloid fibril
Mechanism (biology)
Peptide
Cytotoxicity
Sequence (biology)
Antimicrobial peptides
Chemistry
Biophysics
Biology
Computational biology
Biochemistry
In vitro
Amyloid β
Medicine
Inorganic chemistry
Epistemology
Natural (archaeology)
Disease
Paleontology
Pathology
Philosophy
Metadata
- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.1101/2022.06.23.497336
- https://www.biorxiv.org/content/biorxiv/early/2022/06/23/2022.06.23.497336.full.pdf
- OA Status
- green
- Cited By
- 2
- References
- 82
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4283372451
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4283372451Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1101/2022.06.23.497336Digital Object Identifier
- Title
-
Natural Antimicrobial Peptides Self-assemble as α/β Chameleon AmyloidsWork title
- Type
-
preprintOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2022Year of publication
- Publication date
-
2022-06-23Full publication date if available
- Authors
-
Peleg Ragonis‐Bachar, Bader Rayan, Eilon Barnea, Yizhaq Engelberg, Alexander Upcher, Meytal LandauList of authors in order
- Landing page
-
https://doi.org/10.1101/2022.06.23.497336Publisher landing page
- PDF URL
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https://www.biorxiv.org/content/biorxiv/early/2022/06/23/2022.06.23.497336.full.pdfDirect link to full text PDF
- Open access
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YesWhether a free full text is available
- OA status
-
greenOpen access status per OpenAlex
- OA URL
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https://www.biorxiv.org/content/biorxiv/early/2022/06/23/2022.06.23.497336.full.pdfDirect OA link when available
- Concepts
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Fibril, Creatures, Amyloid (mycology), Amyloid fibril, Mechanism (biology), Peptide, Cytotoxicity, Sequence (biology), Antimicrobial peptides, Chemistry, Biophysics, Biology, Computational biology, Biochemistry, In vitro, Amyloid β, Medicine, Inorganic chemistry, Epistemology, Natural (archaeology), Disease, Paleontology, Pathology, PhilosophyTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
2Total citation count in OpenAlex
- Citations by year (recent)
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2022: 2Per-year citation counts (last 5 years)
- References (count)
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82Number of works referenced by this work
- Related works (count)
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10Other works algorithmically related by OpenAlex
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