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

Abstract 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 distributions for the 1H, 15N and 13C atoms of the backbone and side-chain of the SEM2peptide (49–107) (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-terminal. Also in this work, we used phase-sensitive 2D HSQC 1H-15N experiments measuring longitudinal T1 and transverse T2 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 molecule.