Mutation-based structural modification and dynamics study of amyloid beta peptide (1–42): An in-silico-based analysis to cognize the mechanism of aggregation
Alzheimer's disease is the prevalent cause of premature senility, a progressive mental disorder due to degeneration in brain and deposition of amyloid β peptide (1–42, a misfolded protein) in the form of aggregation that prevails for a prolonged time and obstructs every aspect of life. One of t...
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| Format: | Article |
| Language: | English |
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Elsevier
2016-03-01
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| Series: | Genomics Data |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213596016300010 |
| _version_ | 1818067613149822976 |
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| author | Pritam Kumar Panda Abhaysinha Satish Patil Priyam Patel Hetalkumar Panchal, Dr. |
| author_facet | Pritam Kumar Panda Abhaysinha Satish Patil Priyam Patel Hetalkumar Panchal, Dr. |
| author_sort | Pritam Kumar Panda |
| collection | DOAJ |
| description | Alzheimer's disease is the prevalent cause of premature senility, a progressive mental disorder due to degeneration in brain and deposition of amyloid β peptide (1–42, a misfolded protein) in the form of aggregation that prevails for a prolonged time and obstructs every aspect of life. One of the primary hallmarks of the neuropathological disease is the accretion of amyloid β peptide in the brain that leads to Alzheimer's disease, but the mechanism is still a mystery. Several investigations have shown that mutations at specific positions have a significant impact in stability of the peptide as predicted from aggregation profiles. Here in our study, we have analyzed the mutations by substituting residues at position A22G, E22G, E22K, E22Q, D23N, L34V and molecular dynamics have been performed to check the deviation in stability and conformation of the peptide. The results validated that the mutations at specific positions lead to instability and the proline substitution at E22P and L34P stalled the aggregation of the peptide. Keywords: Amyloid β peptide, Alzheimer's disease, Aggregation, Mutational analysis, NAMD, UCSF Chimera, Discovery Studio Visualizer |
| first_indexed | 2024-12-10T15:26:28Z |
| format | Article |
| id | doaj.art-19a7cb9b14324a809b9a4f0cece64943 |
| institution | Directory Open Access Journal |
| issn | 2213-5960 |
| language | English |
| last_indexed | 2024-12-10T15:26:28Z |
| publishDate | 2016-03-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Genomics Data |
| spelling | doaj.art-19a7cb9b14324a809b9a4f0cece649432022-12-22T01:43:31ZengElsevierGenomics Data2213-59602016-03-017189194Mutation-based structural modification and dynamics study of amyloid beta peptide (1–42): An in-silico-based analysis to cognize the mechanism of aggregationPritam Kumar Panda0Abhaysinha Satish Patil1Priyam Patel2Hetalkumar Panchal, Dr.3School of Biotechnology and Bioinformatics, D.Y. Patil University, Navi Mumbai, India; Corresponding author.School of Biotechnology and Bioinformatics, D.Y. Patil University, Navi Mumbai, IndiaSchool of Biotechnology and Bioinformatics, D.Y. Patil University, Navi Mumbai, IndiaGujarat Agricultural Biotechnology Institute, Navsari Agricultural University, Athwa Farm, Ghod Dod Road, Surat, Gujarat, IndiaAlzheimer's disease is the prevalent cause of premature senility, a progressive mental disorder due to degeneration in brain and deposition of amyloid β peptide (1–42, a misfolded protein) in the form of aggregation that prevails for a prolonged time and obstructs every aspect of life. One of the primary hallmarks of the neuropathological disease is the accretion of amyloid β peptide in the brain that leads to Alzheimer's disease, but the mechanism is still a mystery. Several investigations have shown that mutations at specific positions have a significant impact in stability of the peptide as predicted from aggregation profiles. Here in our study, we have analyzed the mutations by substituting residues at position A22G, E22G, E22K, E22Q, D23N, L34V and molecular dynamics have been performed to check the deviation in stability and conformation of the peptide. The results validated that the mutations at specific positions lead to instability and the proline substitution at E22P and L34P stalled the aggregation of the peptide. Keywords: Amyloid β peptide, Alzheimer's disease, Aggregation, Mutational analysis, NAMD, UCSF Chimera, Discovery Studio Visualizerhttp://www.sciencedirect.com/science/article/pii/S2213596016300010 |
| spellingShingle | Pritam Kumar Panda Abhaysinha Satish Patil Priyam Patel Hetalkumar Panchal, Dr. Mutation-based structural modification and dynamics study of amyloid beta peptide (1–42): An in-silico-based analysis to cognize the mechanism of aggregation Genomics Data |
| title | Mutation-based structural modification and dynamics study of amyloid beta peptide (1–42): An in-silico-based analysis to cognize the mechanism of aggregation |
| title_full | Mutation-based structural modification and dynamics study of amyloid beta peptide (1–42): An in-silico-based analysis to cognize the mechanism of aggregation |
| title_fullStr | Mutation-based structural modification and dynamics study of amyloid beta peptide (1–42): An in-silico-based analysis to cognize the mechanism of aggregation |
| title_full_unstemmed | Mutation-based structural modification and dynamics study of amyloid beta peptide (1–42): An in-silico-based analysis to cognize the mechanism of aggregation |
| title_short | Mutation-based structural modification and dynamics study of amyloid beta peptide (1–42): An in-silico-based analysis to cognize the mechanism of aggregation |
| title_sort | mutation based structural modification and dynamics study of amyloid beta peptide 1 42 an in silico based analysis to cognize the mechanism of aggregation |
| url | http://www.sciencedirect.com/science/article/pii/S2213596016300010 |
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