ACE-Inhibitory and Antioxidant Activity of Temporin-Ra Peptide: Biochemical Characterization and Molecular Modeling Study
Abstract In this study, the inhibitory effect of Temporin-Ra (FP-14 peptide) on angiotensin converting enzyme (ACE) was evaluated. Inhibition mechanism was investigated by kinetic studies and molecular docking simulation. Lineweaver–Burk plot revealed that Temporin-Ra behaved as a non-competitive ACE inhibitor supported by the docking simulation. The $ IC_{50} $ and $ K_{i} $ values were determined to be 22.19 μM and 36 µg/ml, respectively. Molecular docking simulation showed that Temporin-Ra bound to both of N- and C-domains of ACE by forming hydrogen bonds and electrostatic interactions; Temporin-Ra displayed higher affinity to C-domain than N-domain. Antioxidant activity of Temporin-Ra was examined using different methods. The antioxidant activity of Temporin-Ra (0.2 mg/ml) in the inhibition of linoleic acid autoxidation was evaluated to be 57 %. 1,1-diphenyl-2-picrylhydrazyl and 2, 2-azino-bis (3-ethylbenzothiazoline-6-sulphonicacid) diammonium salt radicals scavenging activities were 60 % at 0.5 mg/ml and 37 % at 0.3 mg/ml, respectively. The hydroxyl radical scavenging of FP-14 peptide at 0.33 mg/ml was 55 %. The results suggest that Temporin-Ra is a multifunctional peptide that could be exploited to develop new anti-hypertension drugs and bio-compatible natural antioxidants..
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
2014 |
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| Erschienen: |
2014 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:20 |
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| Enthalten in: |
International journal of peptide research and therapeutics - 20(2014), 4 vom: 16. Juli, Seite 493-500 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Mojallal-Tabatabaei, Zahra [VerfasserIn] |
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| Links: |
Volltext [lizenzpflichtig] |
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| BKL: | |
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| Themen: |
Angiotensin I-converting enzyme |
| Anmerkungen: |
© Springer Science+Business Media New York 2014 |
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| doi: |
10.1007/s10989-014-9416-x |
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| funding: |
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| PPN (Katalog-ID): |
OLC2067152440 |
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| 520 | |a Abstract In this study, the inhibitory effect of Temporin-Ra (FP-14 peptide) on angiotensin converting enzyme (ACE) was evaluated. Inhibition mechanism was investigated by kinetic studies and molecular docking simulation. Lineweaver–Burk plot revealed that Temporin-Ra behaved as a non-competitive ACE inhibitor supported by the docking simulation. The $ IC_{50} $ and $ K_{i} $ values were determined to be 22.19 μM and 36 µg/ml, respectively. Molecular docking simulation showed that Temporin-Ra bound to both of N- and C-domains of ACE by forming hydrogen bonds and electrostatic interactions; Temporin-Ra displayed higher affinity to C-domain than N-domain. Antioxidant activity of Temporin-Ra was examined using different methods. The antioxidant activity of Temporin-Ra (0.2 mg/ml) in the inhibition of linoleic acid autoxidation was evaluated to be 57 %. 1,1-diphenyl-2-picrylhydrazyl and 2, 2-azino-bis (3-ethylbenzothiazoline-6-sulphonicacid) diammonium salt radicals scavenging activities were 60 % at 0.5 mg/ml and 37 % at 0.3 mg/ml, respectively. The hydroxyl radical scavenging of FP-14 peptide at 0.33 mg/ml was 55 %. The results suggest that Temporin-Ra is a multifunctional peptide that could be exploited to develop new anti-hypertension drugs and bio-compatible natural antioxidants. | ||
| 650 | 4 | |a Angiotensin I-converting enzyme | |
| 650 | 4 | |a Antioxidant | |
| 650 | 4 | |a Bioactive peptides | |
| 650 | 4 | |a Molecular modeling | |
| 700 | 1 | |a Asoodeh, Ahmad |4 aut | |
| 700 | 1 | |a Asadi, Fatemeh |4 aut | |
| 700 | 1 | |a Nezafati, Hamid Reza |4 aut | |
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