A study on the delayed effect of tilapia skin collagen on skin aging for mice and its possible mechanism

Pu, Xi; Qu, Yang

doi:10.1111/jocd.15835

Cited by 3 publications

(1 citation statement)

References 14 publications

(22 reference statements)

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“…Furthermore, studies have demonstrated that fish skin collagen is a valuable source of bioactive peptides, characterized by its protein composition and amino acid distribution. Peptides derived from tilapia skin have been found to exhibit antioxidant (Ma et al., 2022), anti‐aging (Pu & Qu, 2023), hypotensive (Chen et al., 2019), hypoglycemic (Liu et al., 2022), and hypolipidemic (Ning et al., 2017) properties. However, few studies on dual inhibitory peptides of ACE and DPP‐IV from tilapia skin have been reported.…”

Section: Introductionmentioning

confidence: 99%

Two novel angiotensin‐converting enzyme (ACE) and dipeptidyl peptidase IV (DPP‐IV) inhibiting peptides from tilapia (Oreochromis mossambicus) skin and their molecular docking mechanism

Chen,

Ji,

Luo

et al. 2024

Journal of Food Science

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In the study, papain was used to hydrolyze tilapia (Oreochromis mossambicus) skin to obtain a tilapia skin hydrolysate (TSH) with dual angiotensin‐converting enzyme (ACE) and dipeptidyl peptidase IV (DPP‐IV) inhibitory activities. The resulting TSH was sequentially fractionated by ultrafiltration, size exclusion separation chromatography, and reverse‐phase high‐performance liquid chromatography. Its inhibitory effects on ACE and DPP‐IV were determined by commercial reagent kits. Two peptides purified from TSH were identified as Gly‐Pro‐Leu‐Gly‐Ala‐Leu (GPLGAL) and Lys‐Pro‐Ala‐Gly‐Asn (KPAGN) by the ultra‐performance liquid chromatography–tandem mass spectrometry (UPLC–MS/MS). Inhibitory concentration (IC50) of GPLGAL on ACE and DPP‐IV were 117.20 ± 1.69 and 187.10 ± 2.75 µM, respectively. IC50 of KPAGN on ACE and DPP‐IV were 137.40 ± 2.33 and 259.20 ± 2.85 µM, respectively. The molecular simulation demonstrated that the binding affinities of GPLGAL to ACE and DPP‐IV proteins were −8.5 and −7.4 kcal/mol, respectively, whereas those of KPAGN to ACE and DPP‐IV proteins were −7.9 and −6.7 kcal/mol, respectively. GPLGAL interacted with 21 amino acid residues of the ACE active site, whereas KPAGN engaged with 19 amino acid residues. Additionally, GPLGAL interacted with 10 amino acid residues of the DPP‐IV active site, whereas KPAGN engaged with 13 amino acid residues. The two peptides predominantly occupied the active sites of ACE (His513, Tyr523, and Ala354) and DPP‐IV (Tyr662 and Arg125) through hydrogen bonding. This leads to the deactivation of ACE and DPP‐IV.Practical ApplicationAccelerate tilapia skin development and high‐value utilization; provide foundation for preparing the peptides with dual ACE and DPP‐IV inhibiting activity.

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Section: Introductionmentioning

confidence: 99%

Two novel angiotensin‐converting enzyme (ACE) and dipeptidyl peptidase IV (DPP‐IV) inhibiting peptides from tilapia (Oreochromis mossambicus) skin and their molecular docking mechanism

Chen,

Ji,

Luo

et al. 2024

Journal of Food Science

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Uncovering key mechanisms and intervention therapies in aging skin

Zhang,

Liu,

Yue

et al. 2024

Cytokine & Growth Factor Reviews

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Recent update: collagen extraction from marine resources as a promising natural antiaging

Isnaini,

Prajaputra,

Syafhira

et al. 2024

BIO Web Conf.

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Aging is a natural process that occurs in every human. Aging can be prevented or slowed down through the appropriate and suitable use of collagen as an anti-aging treatment. Collagen is typically derived from raw materials such as pig or cow bones/skin, but recently there have been frequent outbreaks of infectious diseases among livestock, prompting the exploration of raw materials sourced from the sea to address this issue and create promising collagen for anti-aging purposes. The objective of this literature review research is to explore the potential of collagen extracts from marine resources as an anti-aging solution through an examination of relevant literature, which can serve as a reference for future research. A systematic review method was employed by collecting data from various literature sources, including research journals published both nationally and internationally, which discuss various marine resources containing collagen with anti-aging properties. Based on the systematic review, several natural resources containing collagen with anti-aging properties were identified, including sea cucumbers (Holothuroidea sp.), milkfish (Chanos chanos), tilapia (Oreochromis niloticus), jellyfish (Rhopilema esculentum), starfish (Asterias pectinifera), mackerel (Decapterus macarellus), squid (Todarodes pacificus), silver carp (Hypophthalmichthys molitrix), and blue sharks (Prionace glauca).

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A study on the delayed effect of tilapia skin collagen on skin aging for mice and its possible mechanism

Cited by 3 publications

References 14 publications

Two novel angiotensin‐converting enzyme (ACE) and dipeptidyl peptidase IV (DPP‐IV) inhibiting peptides from tilapia (Oreochromis mossambicus) skin and their molecular docking mechanism

Two novel angiotensin‐converting enzyme (ACE) and dipeptidyl peptidase IV (DPP‐IV) inhibiting peptides from tilapia (Oreochromis mossambicus) skin and their molecular docking mechanism

Uncovering key mechanisms and intervention therapies in aging skin

Recent update: collagen extraction from marine resources as a promising natural antiaging

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