| Форма представления | Статьи в зарубежных журналах и сборниках |
| Год публикации | 2023 |
| Язык | английский |
|
Блохин Дмитрий Сергеевич, автор
|
| Библиографическое описание на языке оригинала |
Osetrina, D.A.; Kusova, A.M.; Bikmullin, A.G.; Klochkova, E.A.; Yulmetov, A.R.; Semenova, E.A.; Mukhametzyanov, T.A.; Usachev, K.S.; Klochkov, V.V.; Blokhin, D.S. Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation. Int. J. Mol. Sci. 2023, 24, 8949. |
| Аннотация |
It is known that four peptide fragments of predominant protein in human semen Semenogelin 1 (SEM1) (SEM1(86–107), SEM1(68–107), SEM1(49–107) and SEM1(45–107)) are involved in fertilization and amyloid formation processes. In this work, the structure and dynamic behavior of SEM1(45–107) and SEM1(49–107) peptides and their N-domains were described. According to ThT fluorescence spectroscopy data, it was shown that the amyloid formation of SEM1(45–107) starts immediately after purification, which is not observed for SEM1(49–107). Seeing that the peptide amino acid sequence of SEM1(45–107) differs from SEM1(49–107) only by the presence of four additional amino acid residues in the N domain, these domains of both peptides were obtained via solid-phase synthesis and the difference in their dynamics and structure was investigated. SEM1(45–67) and SEM1(49–67) showed no principal difference in dynamic behavior in water solution. Furthermore, we obtained mostly disordered structures of SEM1(45–67) and SEM1(49–67). However, SEM1(45–67) contains a helix (E58-K60) and helix-like (S49-Q51) fragments. These helical fragments may rearrange into β-strands during amyloid formation process. Thus, the difference in full-length peptides' (SEM1(45–107) and SEM1(49–107)) amyloid-forming behavior may be explained by the presence of a structured helix at the SEM1(45–107) N-terminus, which contributes to an increased rate of amyloid formation. |
| Ключевые слова |
SEM1(49?107); SEM1(45?107); Semenogelin 1; amyloid; HIV; NMR spectroscopy; CD spectroscopy; DLS spectroscopy; ThT fluorescence; spatial structure |
| Название журнала |
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
|
| URL |
https://www.mdpi.com/1422-0067/24/10/8949 |
| Пожалуйста, используйте этот идентификатор, чтобы цитировать или ссылаться на эту карточку |
https://repository.kpfu.ru/?p_id=299616 |
Полная запись метаданных  |
| Поле DC |
Значение |
Язык |
| dc.contributor.author |
Блохин Дмитрий Сергеевич |
ru_RU |
| dc.date.accessioned |
2023-01-01T00:00:00Z |
ru_RU |
| dc.date.available |
2023-01-01T00:00:00Z |
ru_RU |
| dc.date.issued |
2023 |
ru_RU |
| dc.identifier.citation |
Osetrina, D.A.; Kusova, A.M.; Bikmullin, A.G.; Klochkova, E.A.; Yulmetov, A.R.; Semenova, E.A.; Mukhametzyanov, T.A.; Usachev, K.S.; Klochkov, V.V.; Blokhin, D.S. Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation. Int. J. Mol. Sci. 2023, 24, 8949. |
ru_RU |
| dc.identifier.uri |
https://repository.kpfu.ru/?p_id=299616 |
ru_RU |
| dc.description.abstract |
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES |
ru_RU |
| dc.description.abstract |
It is known that four peptide fragments of predominant protein in human semen Semenogelin 1 (SEM1) (SEM1(86–107), SEM1(68–107), SEM1(49–107) and SEM1(45–107)) are involved in fertilization and amyloid formation processes. In this work, the structure and dynamic behavior of SEM1(45–107) and SEM1(49–107) peptides and their N-domains were described. According to ThT fluorescence spectroscopy data, it was shown that the amyloid formation of SEM1(45–107) starts immediately after purification, which is not observed for SEM1(49–107). Seeing that the peptide amino acid sequence of SEM1(45–107) differs from SEM1(49–107) only by the presence of four additional amino acid residues in the N domain, these domains of both peptides were obtained via solid-phase synthesis and the difference in their dynamics and structure was investigated. SEM1(45–67) and SEM1(49–67) showed no principal difference in dynamic behavior in water solution. Furthermore, we obtained mostly disordered structures of SEM1(45–67) and SEM1(49–67). However, SEM1(45–67) contains a helix (E58-K60) and helix-like (S49-Q51) fragments. These helical fragments may rearrange into β-strands during amyloid formation process. Thus, the difference in full-length peptides' (SEM1(45–107) and SEM1(49–107)) amyloid-forming behavior may be explained by the presence of a structured helix at the SEM1(45–107) N-terminus, which contributes to an increased rate of amyloid formation. |
ru_RU |
| dc.language.iso |
ru |
ru_RU |
| dc.subject |
|
ru_RU |
| dc.title |
Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation |
ru_RU |
| dc.type |
Статьи в зарубежных журналах и сборниках |
ru_RU |
|
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