1 H, 13 C, and 15 N resonance assignments of the amyloidogenic peptide SEM2(49-107) by NMR spectroscopy.

Autor: Troshkina AA; NMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan, 420008, Russia. AnaATroshkina@kpfu.ru., Klochkov VV; NMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan, 420008, Russia., Bikmullin AG; Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlevskaya, Kazan, 420008, Russia., Klochkova EA; Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlevskaya, Kazan, 420008, Russia., Blokhin DS; NMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan, 420008, Russia.; Department of Chemistry and Chemical Biology, TU Dortmund University, 44227, Dortmund, Germany.
Jazyk: angličtina
Zdroj: Biomolecular NMR assignments [Biomol NMR Assign] 2024 Nov 29. Date of Electronic Publication: 2024 Nov 29.
DOI: 10.1007/s12104-024-10209-y
Abstrakt: It has been shown that human seminal fluid is a major factor in enhancing HIV activity. The SEM2(49-107) peptide is a product of cleavage after ejaculation by internal prostheses of the semenogelin 2 protein, expressed in seminal vesicles. It is established that the peptide SEM2(49-107) forms amyloid fibrils, which increase probability of contracting HIV infection. In this nuclear magnetic resonance (NMR) study, we present almost complete (86%) resonance assignments for the 1 H 15 N and 13 C atoms of the backbone and side-chain of the SEM2(49-107) peptide (BioMagResBank accession number 52356). The secondary structure of SEM2(49-107) peptide was estimated by using two approaches, secondary chemical shifts analysis (CSI) and TALOS-N prediction. Analysis of the secondary structure of the SEM2(49-107) peptide using both methods revealed that the peptide contains helical segments at the C-terminus. Also in this work, we used phase-sensitive 2D HSQC 1 H- 15 N experiments measuring longitudinal T 1 and transverse T 2 NMR relaxation times to report predicted secondary structure and backbone dynamics of the SEM2(49-107) peptide. This resonance assignment will form the basis of future NMR research, contributing to a better understanding of the peptide structure and internal dynamics of the molecule.
Competing Interests: Declarations. Competing interests: The authors declare no competing interests.
(© 2024. The Author(s), under exclusive licence to Springer Nature B.V.)
Databáze: MEDLINE
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