ArticleProtein expression and purification2013
Bacterial expression and purification of the amyloidogenic peptide PAPf39 for multidimensional NMR spectroscopy.
Article in Protein expression and purification, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Quantitative detection of amyloid fibrils using fluorescence resonance energy transfer between engineered yellow and cyan proteins.Protein science : a publication of the Protein Society · 2025Article
- Strategies for Optimizing the Production of Proteins and Peptides with Multiple Disulfide Bonds.Antibiotics (Basel, Switzerland) · 2020Review
- Intramolecular diffusion controls aggregation of the PAPf39 peptide.Biophysical chemistry · 2016Article
- Gallic Acid Is an Antagonist of Semen Amyloid Fibrils That Enhance HIV-1 Infection.The Journal of biological chemistry · 2016Article
- K114 (trans, trans)-bromo-2,5-bis(4-hydroxystyryl)benzene is an efficient detector of cationic amyloid fibrils.Protein science : a publication of the Protein Society · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
PAPf39 is a 39 residue peptide fragment from human prostatic acidic phosphatase that forms amyloid fibrils in semen. These fibrils have been implicated in facilitating HIV transmission. To enable structural studies of PAPf39 by NMR spectroscopy, efficient methods allowing the production of milligram quantities of isotopically labeled peptide are essential. Here, we report the high-yield expression and purification of uniformly (13)C- and (15)N-labeled PAPf39 peptide, through expression as a fusion to ubiquitin at the N-terminus and an intein at the C-terminus. This allows the study of the PAPf39 monomer conformational ensemble by NMR spectroscopy. To this end, we performed the NMR chemical shift assignment of the PAPf39 peptide in the monomeric state at low pH.
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