Purification, Identification and Characterization of Antioxidant Peptides from Corn Silk Tryptic Hydrolysate: An Integrated In Vitro-In Silico Approach

Corn silk (CS) is an agro-by-product from corn cultivation. It is used in folk medicines in some countries, besides being commercialized as health-promoting supplements and beverages. Unlike CS-derived natural products, their bioactive peptides, particularly antioxidant peptides, are understudied. T...

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Autores principales: Joe-Hui Ong, Jiun-An Koh, Hui Cao, Sheri-Ann Tan, Fazilah Abd Manan, Fai-Chu Wong, Tsun-Thai Chai
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Publicado: MDPI AG 2021
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spelling oai:doaj.org-article:3a4bbfc8c9a647de81346ee66b1fc7602021-11-25T16:29:07ZPurification, Identification and Characterization of Antioxidant Peptides from Corn Silk Tryptic Hydrolysate: An Integrated In Vitro-In Silico Approach10.3390/antiox101118222076-3921https://doaj.org/article/3a4bbfc8c9a647de81346ee66b1fc7602021-11-01T00:00:00Zhttps://www.mdpi.com/2076-3921/10/11/1822https://doaj.org/toc/2076-3921Corn silk (CS) is an agro-by-product from corn cultivation. It is used in folk medicines in some countries, besides being commercialized as health-promoting supplements and beverages. Unlike CS-derived natural products, their bioactive peptides, particularly antioxidant peptides, are understudied. This study aimed to purify, identify and characterize antioxidant peptides from trypsin-hydrolyzed CS proteins. Purification was accomplished by membrane ultrafiltration, gel filtration chromatography, and strong-cation-exchange solid-phase extraction, guided by 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt radical cation (ABTS<sup>•+</sup>) scavenging, hydrogen peroxide scavenging, and lipid peroxidation inhibition assays. De novo sequencing identified 29 peptides (6–14 residues; 633–1518 Da). The peptides consisted of 33–86% hydrophobic and 10–67% basic residues. Molecular docking found MCFHHHFHK, VHFNKGKKR, and PVVWAAKR having the strongest affinity (−4.7 to −4.8 kcal/mol) to ABTS<sup>•+</sup>, via hydrogen bonds and hydrophobic interactions. Potential cellular mechanisms of the peptides were supported by their interactions with modulators of intracellular oxidant status: Kelch-like ECH-associated protein 1, myeloperoxidase, and xanthine oxidase. NDGPSR (Asn-Asp-Gly-Pro-Ser-Arg), the most promising peptide, showed stable binding to all three cellular targets, besides exhibiting low toxicity, low allergenicity, and cell-penetrating potential. Overall, CS peptides have potential application as natural antioxidant additives and functional food ingredients.Joe-Hui OngJiun-An KohHui CaoSheri-Ann TanFazilah Abd MananFai-Chu WongTsun-Thai ChaiMDPI AGarticleantioxidantin silicoin vitromechanismmolecular dockingpeptideTherapeutics. PharmacologyRM1-950ENAntioxidants, Vol 10, Iss 1822, p 1822 (2021)
institution DOAJ
collection DOAJ
language EN
topic antioxidant
in silico
in vitro
mechanism
molecular docking
peptide
Therapeutics. Pharmacology
RM1-950
spellingShingle antioxidant
in silico
in vitro
mechanism
molecular docking
peptide
Therapeutics. Pharmacology
RM1-950
Joe-Hui Ong
Jiun-An Koh
Hui Cao
Sheri-Ann Tan
Fazilah Abd Manan
Fai-Chu Wong
Tsun-Thai Chai
Purification, Identification and Characterization of Antioxidant Peptides from Corn Silk Tryptic Hydrolysate: An Integrated In Vitro-In Silico Approach
description Corn silk (CS) is an agro-by-product from corn cultivation. It is used in folk medicines in some countries, besides being commercialized as health-promoting supplements and beverages. Unlike CS-derived natural products, their bioactive peptides, particularly antioxidant peptides, are understudied. This study aimed to purify, identify and characterize antioxidant peptides from trypsin-hydrolyzed CS proteins. Purification was accomplished by membrane ultrafiltration, gel filtration chromatography, and strong-cation-exchange solid-phase extraction, guided by 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt radical cation (ABTS<sup>•+</sup>) scavenging, hydrogen peroxide scavenging, and lipid peroxidation inhibition assays. De novo sequencing identified 29 peptides (6–14 residues; 633–1518 Da). The peptides consisted of 33–86% hydrophobic and 10–67% basic residues. Molecular docking found MCFHHHFHK, VHFNKGKKR, and PVVWAAKR having the strongest affinity (−4.7 to −4.8 kcal/mol) to ABTS<sup>•+</sup>, via hydrogen bonds and hydrophobic interactions. Potential cellular mechanisms of the peptides were supported by their interactions with modulators of intracellular oxidant status: Kelch-like ECH-associated protein 1, myeloperoxidase, and xanthine oxidase. NDGPSR (Asn-Asp-Gly-Pro-Ser-Arg), the most promising peptide, showed stable binding to all three cellular targets, besides exhibiting low toxicity, low allergenicity, and cell-penetrating potential. Overall, CS peptides have potential application as natural antioxidant additives and functional food ingredients.
format article
author Joe-Hui Ong
Jiun-An Koh
Hui Cao
Sheri-Ann Tan
Fazilah Abd Manan
Fai-Chu Wong
Tsun-Thai Chai
author_facet Joe-Hui Ong
Jiun-An Koh
Hui Cao
Sheri-Ann Tan
Fazilah Abd Manan
Fai-Chu Wong
Tsun-Thai Chai
author_sort Joe-Hui Ong
title Purification, Identification and Characterization of Antioxidant Peptides from Corn Silk Tryptic Hydrolysate: An Integrated In Vitro-In Silico Approach
title_short Purification, Identification and Characterization of Antioxidant Peptides from Corn Silk Tryptic Hydrolysate: An Integrated In Vitro-In Silico Approach
title_full Purification, Identification and Characterization of Antioxidant Peptides from Corn Silk Tryptic Hydrolysate: An Integrated In Vitro-In Silico Approach
title_fullStr Purification, Identification and Characterization of Antioxidant Peptides from Corn Silk Tryptic Hydrolysate: An Integrated In Vitro-In Silico Approach
title_full_unstemmed Purification, Identification and Characterization of Antioxidant Peptides from Corn Silk Tryptic Hydrolysate: An Integrated In Vitro-In Silico Approach
title_sort purification, identification and characterization of antioxidant peptides from corn silk tryptic hydrolysate: an integrated in vitro-in silico approach
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/3a4bbfc8c9a647de81346ee66b1fc760
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