Amyloidogenic Properties of Peptides Derived from the VHL Tumor Suppressor Protein

Vijay Kumar, Guru Krishna Kumar Viswanathan, Krittika Ralhan, Ehud Gazit, Daniel Segal*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


The von Hippel-Lindau tumor suppressor protein (pVHL) is involved in maintaining cellular oxygen homeostasis through the regulated degradation of HIF-α. The intrinsically disordered nature of pVHL makes it prone to aggregation that impairs its function, and this is further aggravated in mutant versions of the protein, thus promoting tumor development. By using in silico analysis, we predicted six peptide fragments from pVHL to be amyloidogenic. This was verified for two of the peptides by biophysical approaches, which demonstrated self-assembly and formation of β-sheet-rich aggregates, which, under transmission electron microscopy, atomic force microscopy, and X-ray diffraction, displayed typical fibrillar amyloid characteristics. These motifs may serve as proxies for exploring the nature of pVHL aggregation.

Original languageEnglish
Pages (from-to)3565-3568
Number of pages4
Issue number23
StatePublished - 6 Dec 2021


  • Amyloids
  • Cancer
  • Protein aggregation
  • Tumor suppressor protein
  • VHL protein


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