Identification of chlorophyll a-b binding protein AB96 as a novel TGFβ1 neutralizing agent

Sci Rep. 2021 Apr 8;11(1):7740. doi: 10.1038/s41598-021-87454-x.

Abstract

The discovery of compounds and proteins from plants has greatly contributed to modern medicine. Vernonia amygdalina Del. (Compositae) is used by humans and primates for a variety of conditions including parasitic infection. This paper describes the serendipitous discovery that V. amygdalina extract was able to bind to, and functionally inhibit, active TGFβ1. The binding agent was isolated and identified as chlorophyll a-b binding protein AB96. Given that active TGFβ1 contributes to the pathology of many infectious diseases, inhibiting these processes may explain some of the benefits associated with the ingestion of this species. This is the first plant-derived cytokine-neutralizing protein to be described and paves the way for further such discoveries.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Asteraceae / chemistry*
  • Chlorophyll Binding Proteins / chemistry
  • Chlorophyll Binding Proteins / metabolism*
  • Peptides / chemistry
  • Plants, Medicinal
  • Protein Binding
  • Transforming Growth Factor beta1 / antagonists & inhibitors*

Substances

  • Chlorophyll Binding Proteins
  • Peptides
  • Transforming Growth Factor beta1