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Morphology and aggregation of RADA-16-I peptide Studied by AFM, NMR and molecular dynamics simulationsстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 26 августа 2016 г.
- Авторы: Bagrov Dmitry, Gazizova Yuliya, Podgorsky Victor, Udovichenko Igor, Danilkovich Alexey, Prusakov Kirill, Klinov Dmitry
- Журнал: Biopolymers
- Том: 106
- Номер: 1
- Год издания: 2016
- Издательство: John Wiley & Sons Inc.
- Местоположение издательства: United States
- Первая страница: 72
- Последняя страница: 81
- DOI: 10.1002/bip.22755
- Аннотация: RADA-16-I is a self-assembling peptide which forms biocompatible fibrils and hydrogels. We used molecular dynamics simulations, atomic-force microscopy, NMR spectroscopy, and thioflavin T binding assay to examine size, structure, and morphology of RADA-16-I aggregates. We used the native form of RADA-16-I (H-(ArgAlaAspAla)4 -OH) rather than the acetylated one commonly used in the previous studies. At neutral pH, RADA-16-I is mainly in the fibrillar form, the fibrils consist of an even number of stacked β-sheets. At acidic pH, RADA-16-I fibrils disassemble into monomers, which form an amorphous monolayer on graphite and monolayer lamellae on mica. RADA-16-I fibrils were compared with the fibrils of a similar peptide RLDL-16-I. Thickness of β-sheets measured by AFM was in excellent agreement with the molecular dynamics simulations. A pair of RLDL-16-I β-sheets was thicker (2.3 ± 0.4 nm) than a pair of RADA-16-I β-sheets (1.9 ± 0.1 nm) due to the volume difference between alanine and leucine residues.
- Добавил в систему: Багров Дмитрий Владимирович
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Полный текст | Bagrov_et_al-Biopolymers.pdf | 964,7 КБ | 25 июля 2016 [DBagr] |