Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation
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(49–1...
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MDPI AG
2023-05-01
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| Series: | International Journal of Molecular Sciences |
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| author | Daria A. Osetrina Aleksandra M. Kusova Aydar G. Bikmullin Evelina A. Klochkova Aydar R. Yulmetov Evgenia A. Semenova Timur A. Mukhametzyanov Konstantin S. Usachev Vladimir V. Klochkov Dmitriy S. Blokhin |
| author_facet | Daria A. Osetrina Aleksandra M. Kusova Aydar G. Bikmullin Evelina A. Klochkova Aydar R. Yulmetov Evgenia A. Semenova Timur A. Mukhametzyanov Konstantin S. Usachev Vladimir V. Klochkov Dmitriy S. Blokhin |
| author_sort | Daria A. Osetrina |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-11T03:39:41Z |
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| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T03:39:41Z |
| publishDate | 2023-05-01 |
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| spelling | doaj.art-8e41e79393aa4eca85af4ab07ef224912023-11-18T01:44:45ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-05-012410894910.3390/ijms24108949Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid FormationDaria A. Osetrina0Aleksandra M. Kusova1Aydar G. Bikmullin2Evelina A. Klochkova3Aydar R. Yulmetov4Evgenia A. Semenova5Timur A. Mukhametzyanov6Konstantin S. Usachev7Vladimir V. Klochkov8Dmitriy S. Blokhin9NMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan 420008, RussiaNMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan 420008, RussiaNMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan 420008, RussiaNMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan 420008, RussiaNMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan 420008, RussiaNMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan 420008, RussiaNMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan 420008, RussiaLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan 420021, RussiaNMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan 420008, RussiaNMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan 420008, RussiaIt 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.https://www.mdpi.com/1422-0067/24/10/8949SEM1(49–107)SEM1(45–107)Semenogelin 1amyloidHIVNMR spectroscopy |
| spellingShingle | Daria A. Osetrina Aleksandra M. Kusova Aydar G. Bikmullin Evelina A. Klochkova Aydar R. Yulmetov Evgenia A. Semenova Timur A. Mukhametzyanov Konstantin S. Usachev Vladimir V. Klochkov Dmitriy S. Blokhin Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation International Journal of Molecular Sciences SEM1(49–107) SEM1(45–107) Semenogelin 1 amyloid HIV NMR spectroscopy |
| title | Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation |
| title_full | Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation |
| title_fullStr | Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation |
| title_full_unstemmed | Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation |
| title_short | Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation |
| title_sort | extent of n terminus folding of semenogelin 1 cleavage product determines tendency to amyloid formation |
| topic | SEM1(49–107) SEM1(45–107) Semenogelin 1 amyloid HIV NMR spectroscopy |
| url | https://www.mdpi.com/1422-0067/24/10/8949 |
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