On the molecular mechanism of amyloid fibrillogenesis
Amyloid fibrils are known to form out of partially unfolded human lysozyme through self-assembly of its disordered sequences into a cross-β structure. A new molecular mechanism for this process is proposed based on analogies with the mesophase and microsegregation behaviour of copolymers composed of...
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| Published in | Liquid crystals Vol. 33; no. 5; pp. 555 - 558 |
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| Main Author | |
| Format | Journal Article |
| Language | English |
| Published |
Taylor & Francis
01.05.2006
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| Online Access | Get full text |
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| Summary: | Amyloid fibrils are known to form out of partially unfolded human lysozyme through self-assembly of its disordered sequences into a cross-β structure. A new molecular mechanism for this process is proposed based on analogies with the mesophase and microsegregation behaviour of copolymers composed of rigid and flexible blocks. According to the model, α-helical sequences play an essential role on the stabilization of fibrils. The model ought to apply to globular-fibrillar transformations occurring for other proteins and conformational incompatibility might play a role on the stability of native tertiary structures. |
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| ISSN: | 0267-8292 1366-5855 |
| DOI: | 10.1080/02678290500454115 |