Spatial structure of the fibril-forming SEM1(86–107) peptide in a complex with dodecylphosphocholine micelles

Spatial structure of the fibril-forming SEM1(86–107) peptide in a complex with dodecylphosphocholine micelles

The SEM1(86–107) peptide is a fragment of the semenogelin 1 protein, a component of human semen coagulum. The peptide is known to form amyloid fibrils, which increase the infectious activity of the human immunodeficiency virus. In the present work, we determined the spatial structure of the SEM1(86–...

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Bibliographic Details
Published in:Russian chemical bulletin Vol. 70; no. 12; pp. 2422 - 2426
Main Authors: Sanchugova, D. A., Bikmullin, A. G., Klochkov, V. V., Aganov, A. V., Blokhin, D. S.
Format: Journal Article
Language:English
Published: New York Springer US 01-12-2021
Springer Nature B.V
Subjects:
Aqueous solutions
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Fragments
Full Articles
Inorganic Chemistry
Micelles
NMR spectroscopy
Organic Chemistry
Peptides
Semen
spatial structure
SEM1(86–107) peptide
NMR spectroscopy
dodecylphosphocholine micelles
semenogelin 1
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Summary:The SEM1(86–107) peptide is a fragment of the semenogelin 1 protein, a component of human semen coagulum. The peptide is known to form amyloid fibrils, which increase the infectious activity of the human immunodeficiency virus. In the present work, we determined the spatial structure of the SEM1(86–107) peptide in an aqueous solution containing dodecylphosphocholine (DPC) micelles by NMR spectroscopy. It was found that the peptide has a disordered structure with a 3 10 -helix turn (fragment 94T–96S). Despite a disordered structure of the peptide, it was possible to distinguish fragments with good convergence in the ensemble (87L–92K, 94T–97Q, and 104Q–107L). A comparison of the obtained structure with the data on the structure of the SEM1(86–107) peptide in an aqueous solution in the absence of DPC micelles showed that the presence of DPC micelles in an aqueous solution led to the emergence of a helical fragment of the SEM1(86–107) peptide and the change in the distribution of hydrophilic fragments of the molecule.
ISSN:1066-5285
1573-9171
DOI:10.1007/s11172-021-3362-5