Bioactivity of an antihypertensive peptide expressed in Chlamydomonas reinhardtii

J Biotechnol. 2016 Dec 20:240:76-84. doi: 10.1016/j.jbiotec.2016.11.001. Epub 2016 Nov 2.

Abstract

In this study, we developed a transplastomic C. reinhardtii strain that accumulates anti-hypertensive peptides. Tandem repeats of VLPVP peptide were included. PCR analysis confirmed the presence of the transgene in the modified strains. After in vitro digestion of biomass of a recombinant C. reinhardtii strain the VLVPV peptide was identified and quantified by HPLC. The highest expression line produced 0.292mg of recombinant protein per mg of freeze-dried biomass. Intragastric administration of the genetically modified strain to spontaneous hypertensive rats at a dose of 30mg/kg of body weight of recombinant protein significantly reduced systolic blood pressure. At the same dose, the recombinant protein exerts an ACE-inhibitory effect. This is the first study that indicates the potential of this microalga producing an antihypertensive peptide as a dietary supplement for hypertension patients.

Keywords: Bioactive peptides; Hypertension; Microalgae; Spontaneous hypertensive rats.

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors
  • Animals
  • Antihypertensive Agents / pharmacology*
  • Blood Pressure / drug effects
  • Chlamydomonas reinhardtii*
  • Hypertension / drug therapy*
  • Hypertension / physiopathology
  • Male
  • Oligopeptides / biosynthesis
  • Oligopeptides / genetics
  • Oligopeptides / isolation & purification
  • Oligopeptides / pharmacology*
  • Rats
  • Rats, Inbred SHR
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / pharmacology*

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Antihypertensive Agents
  • Oligopeptides
  • Recombinant Proteins
  • valyl-leucyl-prolyl-valyl-proline