期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 24, 期 10, 页码 -出版社
MDPI
DOI: 10.3390/ijms24108949
关键词
SEM1(49-107); SEM1(45-107); Semenogelin 1; amyloid; HIV; NMR spectroscopy; CD spectroscopy; DLS spectroscopy; ThT fluorescence; spatial structure
This study describes the involvement of four peptide fragments of Semenogelin 1 (SEM1) in fertilization and amyloid formation processes. The amyloid formation of SEM1(45-107) was observed immediately after purification, while SEM1(49-107) did not show this behavior. The difference in amyloid-forming behavior between the two peptides can be explained by the presence of a structured helix at the N-terminus of SEM1(45-107).
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 fi-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.
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