VPPIPP and IPPVPP: two hexapeptides innovated to exert antihypertensive activity

Fengyun Ding; Bingjun Qian; Xin Zhao; Shanqi Shen; Yun Deng; Danfeng Wang; Feng Zhang; Zhongquan Sui; Pu Jing

doi:10.1371/journal.pone.0062384

VPPIPP and IPPVPP: two hexapeptides innovated to exert antihypertensive activity

PLoS One. 2013 Apr 30;8(4):e62384. doi: 10.1371/journal.pone.0062384. Print 2013.

Authors

Fengyun Ding¹, Bingjun Qian, Xin Zhao, Shanqi Shen, Yun Deng, Danfeng Wang, Feng Zhang, Zhongquan Sui, Pu Jing

Affiliation

¹ Department of Food Science and Engineering, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, China.

Abstract

In this study, two hexapeptides of IPPVPP and VPPIPP were innovated by using two commercial antihypertensive peptides IPP and VPP as two domains cis-linked and trans-linked, respectively. The IPPVPP and VPPIPP were chemically synthesized and evaluated for the antihypertensive activity in vitro/vivo. The in vitro ACE-inhibitory study showed that VPPIPP (34.71 ± 4.38%) has a significantly stronger activity than that of IPPVPP (13.17 ± 0.25%) at a treatment concentration of 10 µmol/L, but it was weaker than the commercial IPP (56.97 ± 2.40%) (P<0.05). However, VPPIPP, IPPVPP, and IPP lowered the systolic blood pressure by 21 ± 0.9%, 17.4 ± 1.3% and 17.5 ± 0.9%, respectively, in rats at 1.5 mg/kg body weight dosage. The result was consistent with the mRNA level of sarcoplasmic reticulum Ca(2+), Mg(2+) -ATPase Gene (SERCA 2a) in rat hearts. Additionally, VPPIPP and IPPVPP showed no negative impact on blood glycometabolism. The results suggested that the two hexapeptides could be potent bioactive peptides in functional foods for people with high blood pressure.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Angiotensin-Converting Enzyme Inhibitors / chemistry*
Angiotensin-Converting Enzyme Inhibitors / therapeutic use*
Animals
Antihypertensive Agents / chemistry*
Antihypertensive Agents / therapeutic use*
Blood Glucose / metabolism
Blood Pressure / drug effects
Male
Peptides / chemistry*
Peptides / therapeutic use*
Peptidyl-Dipeptidase A / metabolism
Rabbits
Rats
Rats, Inbred SHR
Sarcoplasmic Reticulum Calcium-Transporting ATPases / genetics
Transcriptional Activation / drug effects

Substances

Angiotensin-Converting Enzyme Inhibitors
Antihypertensive Agents
Blood Glucose
Peptides
Peptidyl-Dipeptidase A
Sarcoplasmic Reticulum Calcium-Transporting ATPases

Grants and funding

This research was jointly supported by the Shanghai Municipal Natural Science Foundation (grant no. 11ZR1416200), the National Natural Science Foundation of China (grant no. 31071530), and the Youth Foundation of the School of Agriculture and Biology of Shanghai Jiao Tong University (NQN201001). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.