Amyloid fibrils compared to peptide nanotubes
Prefibrillar oligomeric states and amyloid fibrils of amyloid-forming proteins qualify as nanoparticles. We aim to predict what biophysical and biochemical properties they could share in common with better researched peptide nanotubes. We first describe what is known of amyloid fibrils and prefibril...
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| Published in | Biochimica et biophysica acta Vol. 1840; no. 9; pp. 2944 - 2952 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.09.2014
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| Abstract | Prefibrillar oligomeric states and amyloid fibrils of amyloid-forming proteins qualify as nanoparticles. We aim to predict what biophysical and biochemical properties they could share in common with better researched peptide nanotubes. We first describe what is known of amyloid fibrils and prefibrillar aggregates (oligomers and protofibrils): their structure, mechanisms of formation and putative mechanism of cytotoxicity. In distinction from other neuronal fibrillar constituents, amyloid fibrils are believed to cause pathology, however, some can also be functional. Second, we give a review of known biophysical properties of peptide nanotubes. Finally, we compare properties of these two macromolecular states side by side and discuss which measurements that have already been done with peptide nanotubes could be done with amyloid fibrils as well.
•Biophysical properties of peptide nanotubes•Piezoelectricity•Second harmonic generation•Biophysical properties of amyloid fibrils |
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| AbstractList | Prefibrillar oligomeric states and amyloid fibrils of amyloid-forming proteins qualify as nanoparticles. We aim to predict what biophysical and biochemical properties they could share in common with better researched peptide nanotubes. We first describe what is known of amyloid fibrils and prefibrillar aggregates (oligomers and protofibrils): their structure, mechanisms of formation and putative mechanism of cytotoxicity. In distinction from other neuronal fibrillar constituents, amyloid fibrils are believed to cause pathology, however, some can also be functional. Second, we give a review of known biophysical properties of peptide nanotubes. Finally, we compare properties of these two macromolecular states side by side and discuss which measurements that have already been done with peptide nanotubes could be done with amyloid fibrils as well.Prefibrillar oligomeric states and amyloid fibrils of amyloid-forming proteins qualify as nanoparticles. We aim to predict what biophysical and biochemical properties they could share in common with better researched peptide nanotubes. We first describe what is known of amyloid fibrils and prefibrillar aggregates (oligomers and protofibrils): their structure, mechanisms of formation and putative mechanism of cytotoxicity. In distinction from other neuronal fibrillar constituents, amyloid fibrils are believed to cause pathology, however, some can also be functional. Second, we give a review of known biophysical properties of peptide nanotubes. Finally, we compare properties of these two macromolecular states side by side and discuss which measurements that have already been done with peptide nanotubes could be done with amyloid fibrils as well. Prefibrillar oligomeric states and amyloid fibrils of amyloid-forming proteins qualify as nanoparticles. We aim to predict what biophysical and biochemical properties they could share in common with better researched peptide nanotubes. We first describe what is known of amyloid fibrils and prefibrillar aggregates (oligomers and protofibrils): their structure, mechanisms of formation and putative mechanism of cytotoxicity. In distinction from other neuronal fibrillar constituents, amyloid fibrils are believed to cause pathology, however, some can also be functional. Second, we give a review of known biophysical properties of peptide nanotubes. Finally, we compare properties of these two macromolecular states side by side and discuss which measurements that have already been done with peptide nanotubes could be done with amyloid fibrils as well. •Biophysical properties of peptide nanotubes•Piezoelectricity•Second harmonic generation•Biophysical properties of amyloid fibrils Prefibrillar oligomeric states and amyloid fibrils of amyloid-forming proteins qualify as nanoparticles. We aim to predict what biophysical and biochemical properties they could share in common with better researched peptide nanotubes. We first describe what is known of amyloid fibrils and prefibrillar aggregates (oligomers and protofibrils): their structure, mechanisms of formation and putative mechanism of cytotoxicity. In distinction from other neuronal fibrillar constituents, amyloid fibrils are believed to cause pathology, however, some can also be functional. Second, we give a review of known biophysical properties of peptide nanotubes. Finally, we compare properties of these two macromolecular states side by side and discuss which measurements that have already been done with peptide nanotubes could be done with amyloid fibrils as well. |
| Author | Žerovnik, Eva Žganec, Matjaž |
| Author_xml | – sequence: 1 givenname: Matjaž surname: Zganec fullname: Zganec, Matjaž organization: Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute, Jamova 39, Ljubljana, Slovenia; Faculty of Mathematics and Physics, University of Ljubljana, Jadranska 19, Ljubljana, Slovenia – sequence: 2 givenname: Eva surname: Zerovnik fullname: Zerovnik, Eva email: eva.zerovnik@ijs.si organization: Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute, Jamova 39, Ljubljana, Slovenia; CipKeBip - Center of Excellence for integrated approaches in chemistry and biology of proteins, Jamova 39, 1000 Ljubljana, Slovenia. Electronic address: eva.zerovnik@ijs.si |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24907475$$D View this record in MEDLINE/PubMed |
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| Keywords | Quantum confinement Amyloid fibrils Peptide nanotubes optical properties Toxicity oligomers |
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| Snippet | Prefibrillar oligomeric states and amyloid fibrils of amyloid-forming proteins qualify as nanoparticles. We aim to predict what biophysical and biochemical... |
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| SubjectTerms | amyloid Amyloid - chemistry Amyloid - metabolism Amyloid - ultrastructure Amyloid fibrils cytotoxicity Humans nanoparticles nanotubes Nanotubes - chemistry Nanotubes - ultrastructure neurons oligomers optical properties Peptide nanotubes Quantum confinement Toxicity |
| Title | Amyloid fibrils compared to peptide nanotubes |
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