دورية أكاديمية
Sequence dependent aggregation of peptides and fibril formation.
| العنوان: | Sequence dependent aggregation of peptides and fibril formation. |
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| المؤلفون: | Hung NB; Institute of Physics, Vietnam Academy of Science and Technology, 10 Dao Tan, Ba Dinh, Hanoi, Vietnam., Le DM; Institute of Research and Development, Duy Tan University, K7/25 Quang Trung, Da Nang, Vietnam., Hoang TX; Institute of Physics, Vietnam Academy of Science and Technology, 10 Dao Tan, Ba Dinh, Hanoi, Vietnam. |
| المصدر: | The Journal of chemical physics [J Chem Phys] 2017 Sep 14; Vol. 147 (10), pp. 105102. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Institute of Physics Country of Publication: United States NLM ID: 0375360 Publication Model: Print Cited Medium: Internet ISSN: 1089-7690 (Electronic) Linking ISSN: 00219606 NLM ISO Abbreviation: J Chem Phys Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: New York, NY : American Institute of Physics Original Publication: Lancaster, Pa., American Institute of Physics. |
| مواضيع طبية MeSH: | Models, Chemical*, Peptides/*chemistry, Amino Acid Sequence ; Hydrophobic and Hydrophilic Interactions ; Molecular Dynamics Simulation ; Monte Carlo Method ; Protein Aggregates ; Protein Structure, Secondary ; Structure-Activity Relationship |
| مستخلص: | Deciphering the links between amino acid sequence and amyloid fibril formation is key for understanding protein misfolding diseases. Here we use Monte Carlo simulations to study the aggregation of short peptides in a coarse-grained model with hydrophobic-polar (HP) amino acid sequences and correlated side chain orientations for hydrophobic contacts. A significant heterogeneity is observed in the aggregate structures and in the thermodynamics of aggregation for systems of different HP sequences and different numbers of peptides. Fibril-like ordered aggregates are found for several sequences that contain the common HPH pattern, while other sequences may form helix bundles or disordered aggregates. A wide variation of the aggregation transition temperatures among sequences, even among those of the same hydrophobic fraction, indicates that not all sequences undergo aggregation at a presumable physiological temperature. The transition is found to be the most cooperative for sequences forming fibril-like structures. For a fibril-prone sequence, it is shown that fibril formation follows the nucleation and growth mechanism. Interestingly, a binary mixture of peptides of an aggregation-prone and a non-aggregation-prone sequence shows the association and conversion of the latter to the fibrillar structure. Our study highlights the role of a sequence in selecting fibril-like aggregates and also the impact of a structural template on fibril formation by peptides of unrelated sequences. |
| المشرفين على المادة: | 0 (Peptides) 0 (Protein Aggregates) |
| تواريخ الأحداث: | Date Created: 20170917 Date Completed: 20180619 Latest Revision: 20180620 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1063/1.5001517 |
| PMID: | 28915764 |
| قاعدة البيانات: | MEDLINE |
Find this article in full text from Scitation. | تدمد: | 1089-7690 |
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| DOI: | 10.1063/1.5001517 |