Identification and Screening of Potential ACE2 Activating Peptides from Soybean Protein Isolate Hydrolysate against...

Area of Science:

• Biochemistry
• Vascular Biology
• Nutritional Science

Background:

• Endothelial dysfunction, linked to reduced angiotensin-converting enzyme 2 (ACE2) activity, contributes to vascular system pathologies.
• Soybean protein isolate hydrolysate (SPIH) is explored for its potential to counteract angiotensin II (Ang II)-induced endothelial dysfunction.

Purpose of the Study:

• To investigate the effects of SPIH on Ang II-induced endothelial dysfunction in human umbilical vein endothelial cells (HUVECs).
• To elucidate the underlying mechanisms involving ACE2 activation by SPIH.
• To identify potential ACE2-activating peptides within SPIH.

Main Methods:

• Human umbilical vein endothelial cells (HUVECs) were treated with Ang II and SPIH.
• Cell migration, reactive oxygen species (ROS) levels, and nitric oxide (NO) concentrations were measured.
• ACE2 activity and expression were assessed, along with the effects of an ACE2 inhibitor (MLN-4760).
• Peptidomics and bioinformatics were used to screen for ACE2-activating peptides.

Main Results:

• SPIH attenuated Ang II-induced cell migration and decreased ROS levels, while increasing NO concentration in HUVECs.
• The beneficial effects of SPIH were partially reversed by an ACE2 inhibitor, suggesting ACE2 involvement.
• SPIH significantly increased ACE2 expression and activity.
• Two novel ACE2-activating peptides, IVPQ and IAVPT, were identified from SPIH; IVPQ also increased ACE2 protein expression.

Conclusions:

• SPIH exerts protective effects against Ang II-induced endothelial dysfunction by activating ACE2.
• SPIH-derived peptides, particularly IVPQ, contribute to enhanced ACE2 activity and expression, supporting its antihypertensive potential.
• These findings highlight SPIH as a promising therapeutic agent for vascular health through ACE2 modulation.