» Articles » PMID: 31652543

Improving Health-Promoting Effects of Food-Derived Bioactive Peptides Through Rational Design and Oral Delivery Strategies

Overview
Journal Nutrients
Date 2019 Oct 27
PMID 31652543
Citations 21
Authors
Affiliations
Soon will be listed here.
Abstract

Over the last few decades, scientific interest in food-derived bioactive peptides has grown as an alternative to pharmacological treatments in the control of lifestyle-associated diseases, which represent a serious health problem worldwide. Interest has been directed towards the control of hypertension, the management of type 2 diabetes and oxidative stress. Many food-derived antihypertensive peptides act primarily by inhibiting angiotensin I-converting enzyme (ACE), and to a lesser extent, renin enzyme activities. Antidiabetic peptides mainly inhibit dipeptidyl peptidase-IV (DPP-IV) activity, whereas antioxidant peptides act through inactivation of reactive oxygen species, free radicals scavenging, chelation of pro-oxidative transition metals and promoting the activities of intracellular antioxidant enzymes. However, food-derived bioactive peptides have intrinsic weaknesses, including poor chemical and physical stability and a short circulating plasma half-life that must be addressed for their application as nutraceuticals or in functional foods. This review summarizes the application of common pharmaceutical approaches such as rational design and oral delivery strategies to improve the health-promoting effects of food-derived bioactive peptides. We review the structural requirements of antihypertensive, antidiabetic and antioxidant peptides established by integrated computational methods and provide relevant examples of effective oral delivery systems to enhance solubility, stability and permeability of bioactive peptides.

Citing Articles

Special Issue: "Rational Design and Synthesis of Bioactive Molecules".

Kostova I Int J Mol Sci. 2024; 25(18).

PMID: 39337415 PMC: 11432531. DOI: 10.3390/ijms25189927.


Exploring the impact of encapsulation on the stability and bioactivity of peptides extracted from botanical sources: trends and opportunities.

Perez-Perez V, Jimenez-Martinez C, Gonzalez-Escobar J, Corzo-Rios L Front Chem. 2024; 12:1423500.

PMID: 39050374 PMC: 11266027. DOI: 10.3389/fchem.2024.1423500.


Angiotensin-Converting Enzyme and Renin-Inhibitory Activities of Protein Hydrolysates Produced by Alcalase Hydrolysis of Peanut Protein.

Poddar S, Yu J Int J Mol Sci. 2024; 25(13).

PMID: 39000571 PMC: 11242875. DOI: 10.3390/ijms25137463.


Response Surface Modeling and Optimization of Enzymolysis Parameters for the In Vitro Antidiabetic Activities of Peanut Protein Hydrolysates Prepared Using Two Proteases.

Al-Bukhaiti W, Al-Dalali S, Noman A, Qiu S, Abed S, Qiu S Foods. 2023; 11(20).

PMID: 37431052 PMC: 9602261. DOI: 10.3390/foods11203303.


Recent advances in the development of therapeutic peptides.

Fetse J, Kandel S, Mamani U, Cheng K Trends Pharmacol Sci. 2023; 44(7):425-441.

PMID: 37246037 PMC: 10330351. DOI: 10.1016/j.tips.2023.04.003.


References
1.
Matsui R, Honda R, Kanome M, Hagiwara A, Matsuda Y, Togitani T . Designing antioxidant peptides based on the antioxidant properties of the amino acid side-chains. Food Chem. 2017; 245:750-755. DOI: 10.1016/j.foodchem.2017.11.119. View

2.
Auwal S, Zarei M, Tan C, Basri M, Saari N . Improved In Vivo Efficacy of Anti-Hypertensive Biopeptides Encapsulated in Chitosan Nanoparticles Fabricated by Ionotropic Gelation on Spontaneously Hypertensive Rats. Nanomaterials (Basel). 2017; 7(12). PMC: 5746911. DOI: 10.3390/nano7120421. View

3.
Sarmadi B, Ismail A . Antioxidative peptides from food proteins: a review. Peptides. 2010; 31(10):1949-56. DOI: 10.1016/j.peptides.2010.06.020. View

4.
Kagebayashi T, Kontani N, Yamada Y, Mizushige T, Arai T, Kino K . Novel CCK-dependent vasorelaxing dipeptide, Arg-Phe, decreases blood pressure and food intake in rodents. Mol Nutr Food Res. 2012; 56(9):1456-63. DOI: 10.1002/mnfr.201200168. View

5.
Murray B, FitzGerald R . Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production. Curr Pharm Des. 2007; 13(8):773-91. DOI: 10.2174/138161207780363068. View