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β‐Sheet aggregation of kisspeptin‐10 is stimulated by heparin but inhibited by amphiphiles by Søren B. Nielsen; Magnus Franzmann; Rajiv V. Basaiawmoit; Reinhard Wimmer; Jens D. Mikkelsen; Daniel E. Otzen is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
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## Abstract The murine 10‐residue neurohormone kisspeptin (YNWNSFGLRY) is an important regulator of reproductive behavior and gonadotrophin secretion. It is known to form a random coil in solution, but undergoes a structural change in the presence of membranes although the nature of this change is not fully determined. The peptide's conformational versatility raises the question whether it is also able to form ordered aggregates under physiological conditions, which might be relevant as a storage mechanism. Here we show that heparin induces kisspeptin to form β‐sheet rich amyloid aggregates both at neutral (pH 7.0) and slightly acidic (pH 5.2) conditions. Addition of heparin leads to aggregation after a certain lag phase, irrespective of the time of addition of heparin, indicating that heparin is needed to facilitate the formation of fibrillation nuclei. Aggregation is completely inhibited by submicellar concentrations of zwitterionic and anionic surfactants. Unlike previous reports, our NMR data do not indicate persistent structure in the presence of zwitterionic surfactant micelles. Thus kisspeptin can aggregate under physiologically relevant conditions provided heparin is presen
Who reads β‐Sheet aggregation of kisspeptin‐10 is stimulated by heparin but inhibited by amphiphiles?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Søren B. Nielsen; Magnus Franzmann; Rajiv V. Basaiawmoit; Reinhard Wimmer; Jens D. Mikkelsen; Daniel E. Otzen
- Publisher
- Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)
- Published
- 2010
- Language
- EL
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)