Amyloid-Mediated Mechanisms of Membrane Disruption
Protein aggregation and amyloid formation are pathogenic events underlying the development of an increasingly large number of human diseases named “proteinopathies”. Abnormal accumulation in affected tissues of amyloid β (Aβ) peptide, islet amyloid polypeptide (IAPP), and the prion protein, to menti...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-04-01
|
| Series: | Biophysica |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2673-4125/1/2/11 |
| _version_ | 1827685697308327936 |
|---|---|
| author | Michele F. M. Sciacca Carmelo La Rosa Danilo Milardi |
| author_facet | Michele F. M. Sciacca Carmelo La Rosa Danilo Milardi |
| author_sort | Michele F. M. Sciacca |
| collection | DOAJ |
| description | Protein aggregation and amyloid formation are pathogenic events underlying the development of an increasingly large number of human diseases named “proteinopathies”. Abnormal accumulation in affected tissues of amyloid β (Aβ) peptide, islet amyloid polypeptide (IAPP), and the prion protein, to mention a few, are involved in the occurrence of Alzheimer’s (AD), type 2 diabetes mellitus (T2DM) and prion diseases, respectively. Many reports suggest that the toxic properties of amyloid aggregates are correlated with their ability to damage cell membranes. However, the molecular mechanisms causing toxic amyloid/membrane interactions are still far to be completely elucidated. This review aims at describing the mutual relationships linking abnormal protein conformational transition and self-assembly into amyloid aggregates with membrane damage. A cross-correlated analysis of all these closely intertwined factors is thought to provide valuable insights for a comprehensive molecular description of amyloid diseases and, in turn, the design of effective therapies. |
| first_indexed | 2024-03-10T08:58:10Z |
| format | Article |
| id | doaj.art-241a88cea34240ae80ec460751e5ec40 |
| institution | Directory Open Access Journal |
| issn | 2673-4125 |
| language | English |
| last_indexed | 2024-03-10T08:58:10Z |
| publishDate | 2021-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biophysica |
| spelling | doaj.art-241a88cea34240ae80ec460751e5ec402023-11-22T06:57:09ZengMDPI AGBiophysica2673-41252021-04-011213715610.3390/biophysica1020011Amyloid-Mediated Mechanisms of Membrane DisruptionMichele F. M. Sciacca0Carmelo La Rosa1Danilo Milardi2Consiglio Nazionale delle Ricerche, Istituto di Cristallografia, 95126 Catania, ItalyDepartment of Chemistry, University of Catania, 95125 Catania, ItalyConsiglio Nazionale delle Ricerche, Istituto di Cristallografia, 95126 Catania, ItalyProtein aggregation and amyloid formation are pathogenic events underlying the development of an increasingly large number of human diseases named “proteinopathies”. Abnormal accumulation in affected tissues of amyloid β (Aβ) peptide, islet amyloid polypeptide (IAPP), and the prion protein, to mention a few, are involved in the occurrence of Alzheimer’s (AD), type 2 diabetes mellitus (T2DM) and prion diseases, respectively. Many reports suggest that the toxic properties of amyloid aggregates are correlated with their ability to damage cell membranes. However, the molecular mechanisms causing toxic amyloid/membrane interactions are still far to be completely elucidated. This review aims at describing the mutual relationships linking abnormal protein conformational transition and self-assembly into amyloid aggregates with membrane damage. A cross-correlated analysis of all these closely intertwined factors is thought to provide valuable insights for a comprehensive molecular description of amyloid diseases and, in turn, the design of effective therapies.https://www.mdpi.com/2673-4125/1/2/11amylinlipid bilayerprotein aggregationmisfolding |
| spellingShingle | Michele F. M. Sciacca Carmelo La Rosa Danilo Milardi Amyloid-Mediated Mechanisms of Membrane Disruption Biophysica amylin lipid bilayer protein aggregation misfolding |
| title | Amyloid-Mediated Mechanisms of Membrane Disruption |
| title_full | Amyloid-Mediated Mechanisms of Membrane Disruption |
| title_fullStr | Amyloid-Mediated Mechanisms of Membrane Disruption |
| title_full_unstemmed | Amyloid-Mediated Mechanisms of Membrane Disruption |
| title_short | Amyloid-Mediated Mechanisms of Membrane Disruption |
| title_sort | amyloid mediated mechanisms of membrane disruption |
| topic | amylin lipid bilayer protein aggregation misfolding |
| url | https://www.mdpi.com/2673-4125/1/2/11 |
| work_keys_str_mv | AT michelefmsciacca amyloidmediatedmechanismsofmembranedisruption AT carmelolarosa amyloidmediatedmechanismsofmembranedisruption AT danilomilardi amyloidmediatedmechanismsofmembranedisruption |