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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...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10219109/ https://www.ncbi.nlm.nih.gov/pubmed/37240295 http://dx.doi.org/10.3390/ijms24108949 |
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author | Osetrina, Daria A. Kusova, Aleksandra M. Bikmullin, Aydar G. Klochkova, Evelina A. Yulmetov, Aydar R. Semenova, Evgenia A. Mukhametzyanov, Timur A. Usachev, Konstantin S. Klochkov, Vladimir V. Blokhin, Dmitriy S. |
author_facet | Osetrina, Daria A. Kusova, Aleksandra M. Bikmullin, Aydar G. Klochkova, Evelina A. Yulmetov, Aydar R. Semenova, Evgenia A. Mukhametzyanov, Timur A. Usachev, Konstantin S. Klochkov, Vladimir V. Blokhin, Dmitriy S. |
author_sort | Osetrina, Daria A. |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-10219109 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-102191092023-05-27 Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation Osetrina, Daria A. Kusova, Aleksandra M. Bikmullin, Aydar G. Klochkova, Evelina A. Yulmetov, Aydar R. Semenova, Evgenia A. Mukhametzyanov, Timur A. Usachev, Konstantin S. Klochkov, Vladimir V. Blokhin, Dmitriy S. Int J Mol Sci Article 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. MDPI 2023-05-18 /pmc/articles/PMC10219109/ /pubmed/37240295 http://dx.doi.org/10.3390/ijms24108949 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Osetrina, Daria A. Kusova, Aleksandra M. Bikmullin, Aydar G. Klochkova, Evelina A. Yulmetov, Aydar R. Semenova, Evgenia A. Mukhametzyanov, Timur A. Usachev, Konstantin S. Klochkov, Vladimir V. Blokhin, Dmitriy S. Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation |
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 | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10219109/ https://www.ncbi.nlm.nih.gov/pubmed/37240295 http://dx.doi.org/10.3390/ijms24108949 |
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