ArticleBiochimica et biophysica acta2011
The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.
Article in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 34 citations in OpenAlex.
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
- Mechanistic insights into dimerization and cross-β sheet formation in the HIV-associated amyloidogenic peptide PAP248-286 from unbiased all-atom molecular dynamics simulations.Computational and structural biotechnology journal · 2026Article
- Investigating the Effects of the POPC-POPG Lipid Bilayer Composition on PAP248-286 Binding Using CG Molecular Dynamics Simulations.The journal of physical chemistry. B · 2023Article
- SEVI Inhibits Aβ Amyloid Aggregation by Capping the β-Sheet Elongation Edges.Journal of chemical information and modeling · 2023Article
- Article
- Early stages of misfolding of PAP248-286 at two different pH values: An insight from molecular dynamics simulations.Computational and structural biotechnology journal · 2022Article
- Rapid Formation of Peptide/Lipid Coaggregates by the Amyloidogenic Seminal Peptide PAPBiophysical journal · 2020Article
- Structure, function and antagonism of semen amyloids.Chemical communications (Cambridge, England) · 2018Review
- Sulfonated Compounds Bind with Prostatic Acid Phosphatase (PAPChemistryOpen · 2018Article
- In Situ Investigation of Peptide-Lipid Interaction Between PAP248-286 and Model Cell Membranes.The Journal of membrane biology · 2016Article
- Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives.Journal of diabetes research · 2016Review
- Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson's disease patients.Scientific reports · 2015Article
- Repurposing Hsp104 to Antagonize Seminal Amyloid and Counter HIV Infection.Chemistry & biology · 2015Article
- Morphology-Dependent HIV-Enhancing Effect of Semen-Derived Enhancer of Viral Infection.Biophysical journal · 2015Article
- Fluorescence detection of cationic amyloid fibrils in human semen.Bioorganic & medicinal chemistry letters · 2013Article
- Trifluoroethanol modulates amyloid formation by the all α-helical URN1 FF domain.International journal of molecular sciences · 2013Article
- Lipid composition-dependent membrane fragmentation and pore-forming mechanisms of membrane disruption by pexiganan (MSI-78).Biochemistry · 2013Article
- Inhibition of semen-derived enhancer of virus infection (SEVI) fibrillogenesis by zinc and copper.European biophysics journal : EBJ · 2012Article
- The Surprising Role of Amyloid Fibrils in HIV Infection.Biology · 2012Article
- Site specific interaction of the polyphenol EGCG with the SEVI amyloid precursor peptide PAP(248-286).The journal of physical chemistry. B · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Amyloid fibers in human semen known as SEVI (semen-derived enhancer of viral infection) dramatically increase the infectivity of HIV and other enveloped viruses, which appears to be linked to the promotion of bridging interactions and the neutralization of electrostatic repulsion between the host and the viral cell membranes. The SEVI precursor PAP(248-286) is mostly disordered when bound to detergent micelles, in contrast to the highly α-helical structures found for most amyloid proteins. To determine the origin of this difference, the structures of PAP(248-286) were solved in aqueous solution and with 30% and 50% trifluoroethanol. In solution, pulsed field gradient (PFG)-NMR and (1)H-(1)H NOESY experiments indicate that PAP(248-286) is unfolded to an unusual degree for an amyloidogenic peptide but adopts significantly helical structures in TFE solutions. The clear differences between the structures of PAP(248-286) in TFE and SDS indicate electrostatic interactions play a large role in the folding of the peptide, consistent with the slight degree of penetration of PAP(248-286) into the hydrophobic core of the micelle. This is another noticeable difference between PAP(248-286) and other amyloid peptides, which generally show penetration into at least the headgroup region of the bilayer, and may explain some of the unusual properties of SEVI.
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