AbstractBACKGROUNDProtein‐derived peptide fractions can play a key role in the physiological and metabolic regulation and modulation of the body, which suggests that they could be used as functional ingredients to improve health and to reduce the risk of disease. This work aimed to evaluate the in vitro antithrombotic and anticariogenic bioactivity of hydrolysates and protein fractions obtained from cowpea (Vigna unguiculata) by biocatalysis.RESULTSCowpea protein concentrate was hydrolyzed by sequential action with two enzyme systems, Pepsin‐Pancreatin or Alcalase‐Flavourzyme. There was extensive enzymatic hydrolysis, with degrees of hydrolysis of 34.94% and 81.43% for Pepsin‐Pancreatin and Alcalase‐Flavourzyme, respectively. The degree of hydrolysis for the control treatments, without the addition of the enzymes Pepsin‐Pancreatin and Alcalase‐Flavourzyme was 1.1% and 1.2%, respectively. The hydrolysates were subjected to fractionation by ultrafiltration, with five cut‐off points according to molecular weight (<1, 1–3, 3–5, 5–10 and >10 kDa). The Alcalase‐Flavourzyme hydrolysate led to 100% inhibition of platelet aggregation, while the Pepsin‐Pancreatin hydrolysate showed 77.41% inhibition, but this was approximately 100% in the ultrafiltered fractions. The highest anticariogenic activity was obtained with the Pepsin‐Pancreatin system, with 61.55% and 56.07% for calcium and phosphorus demineralization, respectively.CONCLUSIONHydrolysates and their peptide fractions from Vigna unguiculata exhibited inhibition of platelet aggregation and protection of tooth enamel and have the potential for use in the development of functional products with beneficial health effects. © 2024 Society of Chemical Industry.

01 Jan 2025·Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Structure and functional studies of Avt1, a novel peptide from the sea anemone Aulactinia veratra

Article

Author: Smith, Hayden L. ; Norton, Raymond S ; Albar, Renad A. ; Prentis, Peter J ; Wai, Dorothy C C ; Wai, Dorothy C.C. ; Panyi, Gyorgy ; Albar, Renad A ; Szanto, Tibor G ; Sanches, Karoline ; Smith, Hayden L ; Prentis, Peter J. ; Naseem, Muhammad Umair ; Szanto, Tibor G. ; Norton, Raymond S.

Sea anemones are a rich source of peptide toxins spanning a diverse range of biological activities, typically targeting proteins such as ion channels, receptors and transporters. These peptide toxins and their analogues are usually highly stable and selective for their molecular targets, rendering them of interest as molecular tools, insecticides and therapeutics. Recent transcriptomic and proteomic analyses of the sea anemone Aulactinia veratra identified a novel 28-residue peptide, designated Avt1. Avt1 was produced using solid-phase peptide synthesis, followed by oxidative folding and purification of the folded peptide using reversed-phase high-performance liquid chromatography. The liquid chromatography-mass spectrometry profile of synthetic Avt1 showed a pure peak with molecular mass 6 Da less than that of the reduced form of the peptide, indicating the successful formation of three disulfide bonds. The solution structure determined by NMR revealed that Avt1 adopts an inhibitor cystine knot (ICK) fold, in which a ring is formed by two disulfide bonds with a third disulfide penetrating the ring to create the pseudo-knot. This structure provides ICK peptides with high structural, thermal and proteolytic stability. Consistent with its ICK structure, Avt1 was resistant to proteolysis by trypsin, chymotrypsin and pepsin, although it was not a trypsin inhibitor. Avt1 at 100 nM showed no activity in patch-clamp electrophysiological assays against several mammalian voltage-gated ion channels, but has structural features similar to toxins targeting insect sodium ion channels. Although sequence homologues of Avt1 are found in a number of sea anemones, this is the first representative of this family to be characterised structurally and functionally.

01 Dec 2024·Food Chemistry

A novel ACE inhibitory peptide from Douchi hydrolysate: Stability, inhibition mechanism, and antihypertensive potential in spontaneously hypertensive rats

Article

Author: Li, Jianfei ; Zhu, Haiting ; Tai, Zhiyuan ; Yu, Xiaodong ; Chen, Xiya ; He, Qiyi ; Hu, Haohan ; Zhang, Wenhao

Angiotensin I-converting enzyme (ACE) regulates blood pressure through the renin-angiotensin system. Douchi, a traditional fermented soybean condiment, may have antihypertensive effects, but research on ACE inhibitory peptides from Douchi hydrolysates is limited. We hypothesized that enzymatic treatment could enhance ACE inhibitory peptide diversity and efficacy. We tested ten single enzymes and four combinations, finding pepsin-trypsin-chymotrypsin most effective. Hydrolysates were purified using Sephadex G-15 and reversed-phase HPLC, and peptides were identified via LC-MS/MS. Five peptides (LF, VVF, VGAW, GLFG, NGK) were identified, with VGAW as the most potent ACE inhibitor (IC₅₀ 46.6 ± 5.2 μM) showing excellent thermal and pH stability. Lineweaver-Burk plots confirmed competitive inhibition, and molecular docking revealed eight hydrogen bonds between VGAW and ACE. In hypertensive rats, VGAW significantly reduced blood pressure at 12.5, 25, and 50 mg/kg. These findings highlight Douchi as a source of ACE inhibitory peptides and suggest VGAW as a promising functional food ingredient.

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Indication	Country/Location	Organization	Date
Dyspepsia	CN	Jiangsu Puhua Kesheng Pharmaceutical Co Ltd	01 Jan 1982

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