Identification of novel angiotensin converting enzyme (ACE) inhibitory peptides from Pacific saury: In vivo antihypertensive effect and transport route
Nature food-derived angiotensin converting enzyme inhibitory peptides (ACEIPs) can be potent and safe therapeutics for many medical illnesses, particularly hypertension. In this study, novel ACEIPs were screened and identified from Pacific saury by bio-activity guided approach through ultrafiltratio...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Wang, Shu [verfasserIn] Zhang, Lu [verfasserIn] Wang, Hui [verfasserIn] Hu, Zizi [verfasserIn] Xie, Xing [verfasserIn] Chen, Haiqi [verfasserIn] Tu, Zongcai [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2023 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: International journal of biological macromolecules - New York, NY [u.a.] : Elsevier, 1979, 254 |
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| Übergeordnetes Werk: |
volume:254 |
| DOI / URN: |
10.1016/j.ijbiomac.2023.127196 |
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| Katalog-ID: |
ELV066245648 |
|---|
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| 245 | 1 | 0 | |a Identification of novel angiotensin converting enzyme (ACE) inhibitory peptides from Pacific saury: In vivo antihypertensive effect and transport route |
| 264 | 1 | |c 2023 | |
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| 520 | |a Nature food-derived angiotensin converting enzyme inhibitory peptides (ACEIPs) can be potent and safe therapeutics for many medical illnesses, particularly hypertension. In this study, novel ACEIPs were screened and identified from Pacific saury by bio-activity guided approach through ultrafiltration membrane, Sephadex G-25 and RP-HPLC. The antihypertensive effect of ultrafiltration fraction was confirmed with spontaneous hypertensive rats' (SHRs) model. The peptides sequences of which gave the best activity was identified by Q-Orbitrap-MS/MS and selectively synthesized based on the binding energy of molecular docking. Five peptides VVLASLK, LTLK, LEPWR, ELPPK and LPTEK were synthesized, and the peptide LEPWR (IC50 = 99.5 μM) showed the best ACE inhibitory ability. Furthermore, LEPWR against ACE in a mixed competitive pattern and formed six hydrogen bonds with ACE. Additionally, the apparent permeability coefficient (P app ) of LEPWR was 3.56 ± 0.14 × 10−6 cm/s and paracellular transport across tight junctions was the main pathway across the Caco-2 monolayer. Therefore, the Pacific saury is a good material to prepare ACEIPs, but antihypertensive mechanism of peptide LEPWR on SHRs needs further investigation. | ||
| 650 | 4 | |a ACE inhibitory peptide | |
| 650 | 4 | |a Pacific saury | |
| 650 | 4 | |a Isolation and purification | |
| 650 | 4 | |a Molecular docking | |
| 650 | 4 | |a Caco-2 cell monolayers | |
| 700 | 1 | |a Zhang, Lu |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Hui |e verfasserin |4 aut | |
| 700 | 1 | |a Hu, Zizi |e verfasserin |4 aut | |
| 700 | 1 | |a Xie, Xing |e verfasserin |4 aut | |
| 700 | 1 | |a Chen, Haiqi |e verfasserin |4 aut | |
| 700 | 1 | |a Tu, Zongcai |e verfasserin |4 aut | |
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| 912 | |a GBV_ILN_2232 | ||
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10.1016/j.ijbiomac.2023.127196 doi (DE-627)ELV066245648 (ELSEVIER)S0141-8130(23)04093-X DE-627 ger DE-627 rda eng 540 570 VZ BIODIV DE-30 fid 35.80 bkl 58.30 bkl Wang, Shu verfasserin aut Identification of novel angiotensin converting enzyme (ACE) inhibitory peptides from Pacific saury: In vivo antihypertensive effect and transport route 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nature food-derived angiotensin converting enzyme inhibitory peptides (ACEIPs) can be potent and safe therapeutics for many medical illnesses, particularly hypertension. In this study, novel ACEIPs were screened and identified from Pacific saury by bio-activity guided approach through ultrafiltration membrane, Sephadex G-25 and RP-HPLC. The antihypertensive effect of ultrafiltration fraction was confirmed with spontaneous hypertensive rats' (SHRs) model. The peptides sequences of which gave the best activity was identified by Q-Orbitrap-MS/MS and selectively synthesized based on the binding energy of molecular docking. Five peptides VVLASLK, LTLK, LEPWR, ELPPK and LPTEK were synthesized, and the peptide LEPWR (IC50 = 99.5 μM) showed the best ACE inhibitory ability. Furthermore, LEPWR against ACE in a mixed competitive pattern and formed six hydrogen bonds with ACE. Additionally, the apparent permeability coefficient (P app ) of LEPWR was 3.56 ± 0.14 × 10−6 cm/s and paracellular transport across tight junctions was the main pathway across the Caco-2 monolayer. Therefore, the Pacific saury is a good material to prepare ACEIPs, but antihypertensive mechanism of peptide LEPWR on SHRs needs further investigation. ACE inhibitory peptide Pacific saury Isolation and purification Molecular docking Caco-2 cell monolayers Zhang, Lu verfasserin aut Wang, Hui verfasserin aut Hu, Zizi verfasserin aut Xie, Xing verfasserin aut Chen, Haiqi verfasserin aut Tu, Zongcai verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 254 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:254 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.80 Makromolekulare Chemie VZ 58.30 Biotechnologie VZ AR 254 |
| spelling |
10.1016/j.ijbiomac.2023.127196 doi (DE-627)ELV066245648 (ELSEVIER)S0141-8130(23)04093-X DE-627 ger DE-627 rda eng 540 570 VZ BIODIV DE-30 fid 35.80 bkl 58.30 bkl Wang, Shu verfasserin aut Identification of novel angiotensin converting enzyme (ACE) inhibitory peptides from Pacific saury: In vivo antihypertensive effect and transport route 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nature food-derived angiotensin converting enzyme inhibitory peptides (ACEIPs) can be potent and safe therapeutics for many medical illnesses, particularly hypertension. In this study, novel ACEIPs were screened and identified from Pacific saury by bio-activity guided approach through ultrafiltration membrane, Sephadex G-25 and RP-HPLC. The antihypertensive effect of ultrafiltration fraction was confirmed with spontaneous hypertensive rats' (SHRs) model. The peptides sequences of which gave the best activity was identified by Q-Orbitrap-MS/MS and selectively synthesized based on the binding energy of molecular docking. Five peptides VVLASLK, LTLK, LEPWR, ELPPK and LPTEK were synthesized, and the peptide LEPWR (IC50 = 99.5 μM) showed the best ACE inhibitory ability. Furthermore, LEPWR against ACE in a mixed competitive pattern and formed six hydrogen bonds with ACE. Additionally, the apparent permeability coefficient (P app ) of LEPWR was 3.56 ± 0.14 × 10−6 cm/s and paracellular transport across tight junctions was the main pathway across the Caco-2 monolayer. Therefore, the Pacific saury is a good material to prepare ACEIPs, but antihypertensive mechanism of peptide LEPWR on SHRs needs further investigation. ACE inhibitory peptide Pacific saury Isolation and purification Molecular docking Caco-2 cell monolayers Zhang, Lu verfasserin aut Wang, Hui verfasserin aut Hu, Zizi verfasserin aut Xie, Xing verfasserin aut Chen, Haiqi verfasserin aut Tu, Zongcai verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 254 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:254 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.80 Makromolekulare Chemie VZ 58.30 Biotechnologie VZ AR 254 |
| allfields_unstemmed |
10.1016/j.ijbiomac.2023.127196 doi (DE-627)ELV066245648 (ELSEVIER)S0141-8130(23)04093-X DE-627 ger DE-627 rda eng 540 570 VZ BIODIV DE-30 fid 35.80 bkl 58.30 bkl Wang, Shu verfasserin aut Identification of novel angiotensin converting enzyme (ACE) inhibitory peptides from Pacific saury: In vivo antihypertensive effect and transport route 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nature food-derived angiotensin converting enzyme inhibitory peptides (ACEIPs) can be potent and safe therapeutics for many medical illnesses, particularly hypertension. In this study, novel ACEIPs were screened and identified from Pacific saury by bio-activity guided approach through ultrafiltration membrane, Sephadex G-25 and RP-HPLC. The antihypertensive effect of ultrafiltration fraction was confirmed with spontaneous hypertensive rats' (SHRs) model. The peptides sequences of which gave the best activity was identified by Q-Orbitrap-MS/MS and selectively synthesized based on the binding energy of molecular docking. Five peptides VVLASLK, LTLK, LEPWR, ELPPK and LPTEK were synthesized, and the peptide LEPWR (IC50 = 99.5 μM) showed the best ACE inhibitory ability. Furthermore, LEPWR against ACE in a mixed competitive pattern and formed six hydrogen bonds with ACE. Additionally, the apparent permeability coefficient (P app ) of LEPWR was 3.56 ± 0.14 × 10−6 cm/s and paracellular transport across tight junctions was the main pathway across the Caco-2 monolayer. Therefore, the Pacific saury is a good material to prepare ACEIPs, but antihypertensive mechanism of peptide LEPWR on SHRs needs further investigation. ACE inhibitory peptide Pacific saury Isolation and purification Molecular docking Caco-2 cell monolayers Zhang, Lu verfasserin aut Wang, Hui verfasserin aut Hu, Zizi verfasserin aut Xie, Xing verfasserin aut Chen, Haiqi verfasserin aut Tu, Zongcai verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 254 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:254 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.80 Makromolekulare Chemie VZ 58.30 Biotechnologie VZ AR 254 |
| allfieldsGer |
10.1016/j.ijbiomac.2023.127196 doi (DE-627)ELV066245648 (ELSEVIER)S0141-8130(23)04093-X DE-627 ger DE-627 rda eng 540 570 VZ BIODIV DE-30 fid 35.80 bkl 58.30 bkl Wang, Shu verfasserin aut Identification of novel angiotensin converting enzyme (ACE) inhibitory peptides from Pacific saury: In vivo antihypertensive effect and transport route 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nature food-derived angiotensin converting enzyme inhibitory peptides (ACEIPs) can be potent and safe therapeutics for many medical illnesses, particularly hypertension. In this study, novel ACEIPs were screened and identified from Pacific saury by bio-activity guided approach through ultrafiltration membrane, Sephadex G-25 and RP-HPLC. The antihypertensive effect of ultrafiltration fraction was confirmed with spontaneous hypertensive rats' (SHRs) model. The peptides sequences of which gave the best activity was identified by Q-Orbitrap-MS/MS and selectively synthesized based on the binding energy of molecular docking. Five peptides VVLASLK, LTLK, LEPWR, ELPPK and LPTEK were synthesized, and the peptide LEPWR (IC50 = 99.5 μM) showed the best ACE inhibitory ability. Furthermore, LEPWR against ACE in a mixed competitive pattern and formed six hydrogen bonds with ACE. Additionally, the apparent permeability coefficient (P app ) of LEPWR was 3.56 ± 0.14 × 10−6 cm/s and paracellular transport across tight junctions was the main pathway across the Caco-2 monolayer. Therefore, the Pacific saury is a good material to prepare ACEIPs, but antihypertensive mechanism of peptide LEPWR on SHRs needs further investigation. ACE inhibitory peptide Pacific saury Isolation and purification Molecular docking Caco-2 cell monolayers Zhang, Lu verfasserin aut Wang, Hui verfasserin aut Hu, Zizi verfasserin aut Xie, Xing verfasserin aut Chen, Haiqi verfasserin aut Tu, Zongcai verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 254 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:254 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.80 Makromolekulare Chemie VZ 58.30 Biotechnologie VZ AR 254 |
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10.1016/j.ijbiomac.2023.127196 doi (DE-627)ELV066245648 (ELSEVIER)S0141-8130(23)04093-X DE-627 ger DE-627 rda eng 540 570 VZ BIODIV DE-30 fid 35.80 bkl 58.30 bkl Wang, Shu verfasserin aut Identification of novel angiotensin converting enzyme (ACE) inhibitory peptides from Pacific saury: In vivo antihypertensive effect and transport route 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nature food-derived angiotensin converting enzyme inhibitory peptides (ACEIPs) can be potent and safe therapeutics for many medical illnesses, particularly hypertension. In this study, novel ACEIPs were screened and identified from Pacific saury by bio-activity guided approach through ultrafiltration membrane, Sephadex G-25 and RP-HPLC. The antihypertensive effect of ultrafiltration fraction was confirmed with spontaneous hypertensive rats' (SHRs) model. The peptides sequences of which gave the best activity was identified by Q-Orbitrap-MS/MS and selectively synthesized based on the binding energy of molecular docking. Five peptides VVLASLK, LTLK, LEPWR, ELPPK and LPTEK were synthesized, and the peptide LEPWR (IC50 = 99.5 μM) showed the best ACE inhibitory ability. Furthermore, LEPWR against ACE in a mixed competitive pattern and formed six hydrogen bonds with ACE. Additionally, the apparent permeability coefficient (P app ) of LEPWR was 3.56 ± 0.14 × 10−6 cm/s and paracellular transport across tight junctions was the main pathway across the Caco-2 monolayer. Therefore, the Pacific saury is a good material to prepare ACEIPs, but antihypertensive mechanism of peptide LEPWR on SHRs needs further investigation. ACE inhibitory peptide Pacific saury Isolation and purification Molecular docking Caco-2 cell monolayers Zhang, Lu verfasserin aut Wang, Hui verfasserin aut Hu, Zizi verfasserin aut Xie, Xing verfasserin aut Chen, Haiqi verfasserin aut Tu, Zongcai verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 254 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:254 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.80 Makromolekulare Chemie VZ 58.30 Biotechnologie VZ AR 254 |
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ACE inhibitory peptide Pacific saury Isolation and purification Molecular docking Caco-2 cell monolayers |
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Wang, Shu @@aut@@ Zhang, Lu @@aut@@ Wang, Hui @@aut@@ Hu, Zizi @@aut@@ Xie, Xing @@aut@@ Chen, Haiqi @@aut@@ Tu, Zongcai @@aut@@ |
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Wang, Shu |
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Wang, Shu ddc 540 fid BIODIV bkl 35.80 bkl 58.30 misc ACE inhibitory peptide misc Pacific saury misc Isolation and purification misc Molecular docking misc Caco-2 cell monolayers Identification of novel angiotensin converting enzyme (ACE) inhibitory peptides from Pacific saury: In vivo antihypertensive effect and transport route |
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540 570 VZ BIODIV DE-30 fid 35.80 bkl 58.30 bkl Identification of novel angiotensin converting enzyme (ACE) inhibitory peptides from Pacific saury: In vivo antihypertensive effect and transport route ACE inhibitory peptide Pacific saury Isolation and purification Molecular docking Caco-2 cell monolayers |
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Identification of novel angiotensin converting enzyme (ACE) inhibitory peptides from Pacific saury: In vivo antihypertensive effect and transport route |
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Identification of novel angiotensin converting enzyme (ACE) inhibitory peptides from Pacific saury: In vivo antihypertensive effect and transport route |
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identification of novel angiotensin converting enzyme (ace) inhibitory peptides from pacific saury: in vivo antihypertensive effect and transport route |
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Identification of novel angiotensin converting enzyme (ACE) inhibitory peptides from Pacific saury: In vivo antihypertensive effect and transport route |
| abstract |
Nature food-derived angiotensin converting enzyme inhibitory peptides (ACEIPs) can be potent and safe therapeutics for many medical illnesses, particularly hypertension. In this study, novel ACEIPs were screened and identified from Pacific saury by bio-activity guided approach through ultrafiltration membrane, Sephadex G-25 and RP-HPLC. The antihypertensive effect of ultrafiltration fraction was confirmed with spontaneous hypertensive rats' (SHRs) model. The peptides sequences of which gave the best activity was identified by Q-Orbitrap-MS/MS and selectively synthesized based on the binding energy of molecular docking. Five peptides VVLASLK, LTLK, LEPWR, ELPPK and LPTEK were synthesized, and the peptide LEPWR (IC50 = 99.5 μM) showed the best ACE inhibitory ability. Furthermore, LEPWR against ACE in a mixed competitive pattern and formed six hydrogen bonds with ACE. Additionally, the apparent permeability coefficient (P app ) of LEPWR was 3.56 ± 0.14 × 10−6 cm/s and paracellular transport across tight junctions was the main pathway across the Caco-2 monolayer. Therefore, the Pacific saury is a good material to prepare ACEIPs, but antihypertensive mechanism of peptide LEPWR on SHRs needs further investigation. |
| abstractGer |
Nature food-derived angiotensin converting enzyme inhibitory peptides (ACEIPs) can be potent and safe therapeutics for many medical illnesses, particularly hypertension. In this study, novel ACEIPs were screened and identified from Pacific saury by bio-activity guided approach through ultrafiltration membrane, Sephadex G-25 and RP-HPLC. The antihypertensive effect of ultrafiltration fraction was confirmed with spontaneous hypertensive rats' (SHRs) model. The peptides sequences of which gave the best activity was identified by Q-Orbitrap-MS/MS and selectively synthesized based on the binding energy of molecular docking. Five peptides VVLASLK, LTLK, LEPWR, ELPPK and LPTEK were synthesized, and the peptide LEPWR (IC50 = 99.5 μM) showed the best ACE inhibitory ability. Furthermore, LEPWR against ACE in a mixed competitive pattern and formed six hydrogen bonds with ACE. Additionally, the apparent permeability coefficient (P app ) of LEPWR was 3.56 ± 0.14 × 10−6 cm/s and paracellular transport across tight junctions was the main pathway across the Caco-2 monolayer. Therefore, the Pacific saury is a good material to prepare ACEIPs, but antihypertensive mechanism of peptide LEPWR on SHRs needs further investigation. |
| abstract_unstemmed |
Nature food-derived angiotensin converting enzyme inhibitory peptides (ACEIPs) can be potent and safe therapeutics for many medical illnesses, particularly hypertension. In this study, novel ACEIPs were screened and identified from Pacific saury by bio-activity guided approach through ultrafiltration membrane, Sephadex G-25 and RP-HPLC. The antihypertensive effect of ultrafiltration fraction was confirmed with spontaneous hypertensive rats' (SHRs) model. The peptides sequences of which gave the best activity was identified by Q-Orbitrap-MS/MS and selectively synthesized based on the binding energy of molecular docking. Five peptides VVLASLK, LTLK, LEPWR, ELPPK and LPTEK were synthesized, and the peptide LEPWR (IC50 = 99.5 μM) showed the best ACE inhibitory ability. Furthermore, LEPWR against ACE in a mixed competitive pattern and formed six hydrogen bonds with ACE. Additionally, the apparent permeability coefficient (P app ) of LEPWR was 3.56 ± 0.14 × 10−6 cm/s and paracellular transport across tight junctions was the main pathway across the Caco-2 monolayer. Therefore, the Pacific saury is a good material to prepare ACEIPs, but antihypertensive mechanism of peptide LEPWR on SHRs needs further investigation. |
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Identification of novel angiotensin converting enzyme (ACE) inhibitory peptides from Pacific saury: In vivo antihypertensive effect and transport route |
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| score |
7.401043 |