Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State
Amyloid fibril formation is associated with several amyloidoses, including neurodegenerative Alzheimer’s or Parkinson’s diseases. The process of such fibrillar structure formation is still not fully understood, with new mechanistic insights appearing on a regular basis. This, in turn, has limited th...
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| Format: | Article |
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MDPI AG
2022-05-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/10/5421 |
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| author | Kamile Mikalauskaite Mantas Ziaunys Vytautas Smirnovas |
| author_facet | Kamile Mikalauskaite Mantas Ziaunys Vytautas Smirnovas |
| author_sort | Kamile Mikalauskaite |
| collection | DOAJ |
| description | Amyloid fibril formation is associated with several amyloidoses, including neurodegenerative Alzheimer’s or Parkinson’s diseases. The process of such fibrillar structure formation is still not fully understood, with new mechanistic insights appearing on a regular basis. This, in turn, has limited the development of potential anti-amyloid compounds, with only a handful of effective cures or treatment modalities available. One of the multiple amyloid aggregation factors that requires further examination is the ability of proteins to form multiple, structurally distinct aggregates, based on the environmental conditions. In this work, we examine how the initial folding state affects the fibrilization of lysozyme—an amyloidogenic protein, often used in protein aggregation studies. We show that there is a correlation between the initial state of the protein and the aggregate formation lag time, rate of elongation, resulting aggregate structural variability and dye-binding properties, as well as formation lag time and rate of elongation. |
| first_indexed | 2024-03-10T03:45:23Z |
| format | Article |
| id | doaj.art-6babb21f3b1f439bb84c0afd2579a313 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T03:45:23Z |
| publishDate | 2022-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-6babb21f3b1f439bb84c0afd2579a3132023-11-23T11:22:19ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-05-012310542110.3390/ijms23105421Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding StateKamile Mikalauskaite0Mantas Ziaunys1Vytautas Smirnovas2Institute of Biotechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, LithuaniaInstitute of Biotechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, LithuaniaInstitute of Biotechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, LithuaniaAmyloid fibril formation is associated with several amyloidoses, including neurodegenerative Alzheimer’s or Parkinson’s diseases. The process of such fibrillar structure formation is still not fully understood, with new mechanistic insights appearing on a regular basis. This, in turn, has limited the development of potential anti-amyloid compounds, with only a handful of effective cures or treatment modalities available. One of the multiple amyloid aggregation factors that requires further examination is the ability of proteins to form multiple, structurally distinct aggregates, based on the environmental conditions. In this work, we examine how the initial folding state affects the fibrilization of lysozyme—an amyloidogenic protein, often used in protein aggregation studies. We show that there is a correlation between the initial state of the protein and the aggregate formation lag time, rate of elongation, resulting aggregate structural variability and dye-binding properties, as well as formation lag time and rate of elongation.https://www.mdpi.com/1422-0067/23/10/5421amyloidprotein aggregationlysozymefibril |
| spellingShingle | Kamile Mikalauskaite Mantas Ziaunys Vytautas Smirnovas Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State International Journal of Molecular Sciences amyloid protein aggregation lysozyme fibril |
| title | Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State |
| title_full | Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State |
| title_fullStr | Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State |
| title_full_unstemmed | Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State |
| title_short | Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State |
| title_sort | lysozyme amyloid fibril structural variability dependence on initial protein folding state |
| topic | amyloid protein aggregation lysozyme fibril |
| url | https://www.mdpi.com/1422-0067/23/10/5421 |
| work_keys_str_mv | AT kamilemikalauskaite lysozymeamyloidfibrilstructuralvariabilitydependenceoninitialproteinfoldingstate AT mantasziaunys lysozymeamyloidfibrilstructuralvariabilitydependenceoninitialproteinfoldingstate AT vytautassmirnovas lysozymeamyloidfibrilstructuralvariabilitydependenceoninitialproteinfoldingstate |