Roles of Tryptophan and Charged Residues on the Polymorphisms of Amyloids Formed by K-Peptides of Hen Egg White Lysozyme Investigated through Molecular Dynamics Simulations
Abstract
:1. Introduction
2. Results and Discussions
2.1. Disruption of the Antiparallel Beta Amyloid with a Negative Charge Addition
2.2. Antiparallel Beta Amyloid Models Displayed Greater Compactness and Stability
2.3. Antiparallel Amyloid Models of K-Peptides and STDY-K-Peptide at pH 2 Displayed Stretched and Ordered Chains
2.4. Roles of Trp62 Capping the Ends of Highly Ordered Amyloid Models
3. Materials and Methods
3.1. Beta Amyloid Model Creation
3.2. Atomistic Molecular Dynamics Simulations
3.3. Conformational and Interaction Analysis
4. Conclusions
Author Contributions
Funding
Acknowledgments
Conflicts of Interest
References
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Name | Sequence | Asp Protonation | Orientation | No. of Strands | No. of Sheets |
---|---|---|---|---|---|
54–62-AP | GILQINSRW | N/A | Antiparallel | 8 | 2 |
50–62-AP | STDYGILQINSRW | No | Antiparallel | 8 | 2 |
50–62-pH2-AP | STDYGILQINSRW | Yes | Antiparallel | 8 | 2 |
54–62-P | GILQINSRW | N/A | Parallel | 8 | 2 |
50–62-P | STDYGILQINSRW | No | Parallel | 8 | 2 |
50–62-pH2-P | STDYGILQINSRW | Yes | Parallel | 8 | 2 |
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Zein, H.F.; Sutthibutpong, T. Roles of Tryptophan and Charged Residues on the Polymorphisms of Amyloids Formed by K-Peptides of Hen Egg White Lysozyme Investigated through Molecular Dynamics Simulations. Int. J. Mol. Sci. 2023, 24, 2626. https://doi.org/10.3390/ijms24032626
Zein HF, Sutthibutpong T. Roles of Tryptophan and Charged Residues on the Polymorphisms of Amyloids Formed by K-Peptides of Hen Egg White Lysozyme Investigated through Molecular Dynamics Simulations. International Journal of Molecular Sciences. 2023; 24(3):2626. https://doi.org/10.3390/ijms24032626
Chicago/Turabian StyleZein, Husnul Fuad, and Thana Sutthibutpong. 2023. "Roles of Tryptophan and Charged Residues on the Polymorphisms of Amyloids Formed by K-Peptides of Hen Egg White Lysozyme Investigated through Molecular Dynamics Simulations" International Journal of Molecular Sciences 24, no. 3: 2626. https://doi.org/10.3390/ijms24032626