KFU. Card publication. Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation

KAZAN
FEDERAL UNIVERSITY

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- 中文
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EXTENT OF N-TERMINUS FOLDING OF SEMENOGELIN 1 CLEAVAGE PRODUCT DETERMINES TENDENCY TO AMYLOID FORMATION

Form of presentation

Articles in international journals and collections

Year of publication

2023

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Authors, employees of KFU

Blokhin Dmitriy Sergeevich, author

Bibliographic description in the original language

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.

Annotation

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.

Keywords

SEM1(49?107); SEM1(45?107); Semenogelin 1; amyloid; HIV; NMR spectroscopy; CD spectroscopy; DLS spectroscopy; ThT fluorescence; spatial structure

The name of the journal

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

URL

https://www.mdpi.com/1422-0067/24/10/8949

Please use this ID to quote from or refer to the card

https://repository.kpfu.ru/eng/?p_id=299616&p_lang=2

Full metadata record

Field DC	Value	Language
dc.contributor.author	Blokhin Dmitriy Sergeevich	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/eng/?p_id=299616&p_lang=2	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	Articles in international journals and collections	ru_RU