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Characterization of an antihypertensive angiotensin I-converting enzyme inhibitory peptide from the edible mushroom Hypsizygus marmoreus.

Kang MG, Kim YH, Bolormaa Z, Kim MK, Seo GS, Lee JS - Biomed Res Int (2013)

Bottom Line: Therefore, the development of new antihypertensive drugs or bioactive compounds is very important to remedy or prevent hypertension.The purified ACE inhibitor was found to be a new oligopeptide with the sequence LSMGSASLSP.Its molecular weight was estimated to be 567.3 Da and the water extracts containing ACE inhibitor from Hypsizygus marmoreus showed a clear antihypertensive action a spontaneously hypertensive rat.

View Article: PubMed Central - PubMed

Affiliation: Department of Biomedicinal Science and Biotechnology, PaiChai University, Daejeon 302-735, Republic of Korea.

ABSTRACT
Hypertension is one of the very serious diseases and, recently, hypertensive patient longevity has been increased significantly. Therefore, the development of new antihypertensive drugs or bioactive compounds is very important to remedy or prevent hypertension. The antihypertensive angiotensin I-converting enzyme (ACE) inhibitor in water extracts from the brown-cultivar-fruiting-body of Hypsizygus marmoreus was purified with ultrafiltration, C18 solid phase extraction chromatography and reverse-phase HPLC, and the purified ACE inhibitor with inhibitory activity of IC50 value of 0.19 mg/mL was obtained. The purified ACE inhibitor was found to be a new oligopeptide with the sequence LSMGSASLSP. Its molecular weight was estimated to be 567.3 Da and the water extracts containing ACE inhibitor from Hypsizygus marmoreus showed a clear antihypertensive action a spontaneously hypertensive rat.

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Amino acid sequence of the purified oligopeptide (P-1) from H. marmoreus by LC-MS/MS. MS/MS experiments were performed on a LCQ-Deca ESI ion trap mass spectrometer (Thermo Finnigan Co., USA). For protein identification, the MS/MS spectra were searched using SEQUEST (ver 3.3) software. (P-1, TTENVLFG).
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fig2: Amino acid sequence of the purified oligopeptide (P-1) from H. marmoreus by LC-MS/MS. MS/MS experiments were performed on a LCQ-Deca ESI ion trap mass spectrometer (Thermo Finnigan Co., USA). For protein identification, the MS/MS spectra were searched using SEQUEST (ver 3.3) software. (P-1, TTENVLFG).

Mentions: The purified ACE inhibitor was analyzed by LC-MS/MS and three kinds of oligopeptide (i.e., TTENVLFG (P-1), LSMGSASLSP (P-2) and LVNDLVTPVFDNL (P-3)) were obtained (Figures 2, 3, and 4). After chemically synthesizing these three oligopeptides, their ACE inhibitory activities were determined. Chemically synthesized oligopeptides had inhibitory activity (IC50) of 3.03 mg/mL (P-1), 0.19 mg/mL (P-2) and 4.00 mg/mL (P-3), respectively. Thus, we successfully identified the P-2 oligopeptide as the purified ACE inhibitor.


Characterization of an antihypertensive angiotensin I-converting enzyme inhibitory peptide from the edible mushroom Hypsizygus marmoreus.

Kang MG, Kim YH, Bolormaa Z, Kim MK, Seo GS, Lee JS - Biomed Res Int (2013)

Amino acid sequence of the purified oligopeptide (P-1) from H. marmoreus by LC-MS/MS. MS/MS experiments were performed on a LCQ-Deca ESI ion trap mass spectrometer (Thermo Finnigan Co., USA). For protein identification, the MS/MS spectra were searched using SEQUEST (ver 3.3) software. (P-1, TTENVLFG).
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3860087&req=5

fig2: Amino acid sequence of the purified oligopeptide (P-1) from H. marmoreus by LC-MS/MS. MS/MS experiments were performed on a LCQ-Deca ESI ion trap mass spectrometer (Thermo Finnigan Co., USA). For protein identification, the MS/MS spectra were searched using SEQUEST (ver 3.3) software. (P-1, TTENVLFG).
Mentions: The purified ACE inhibitor was analyzed by LC-MS/MS and three kinds of oligopeptide (i.e., TTENVLFG (P-1), LSMGSASLSP (P-2) and LVNDLVTPVFDNL (P-3)) were obtained (Figures 2, 3, and 4). After chemically synthesizing these three oligopeptides, their ACE inhibitory activities were determined. Chemically synthesized oligopeptides had inhibitory activity (IC50) of 3.03 mg/mL (P-1), 0.19 mg/mL (P-2) and 4.00 mg/mL (P-3), respectively. Thus, we successfully identified the P-2 oligopeptide as the purified ACE inhibitor.

Bottom Line: Therefore, the development of new antihypertensive drugs or bioactive compounds is very important to remedy or prevent hypertension.The purified ACE inhibitor was found to be a new oligopeptide with the sequence LSMGSASLSP.Its molecular weight was estimated to be 567.3 Da and the water extracts containing ACE inhibitor from Hypsizygus marmoreus showed a clear antihypertensive action a spontaneously hypertensive rat.

View Article: PubMed Central - PubMed

Affiliation: Department of Biomedicinal Science and Biotechnology, PaiChai University, Daejeon 302-735, Republic of Korea.

ABSTRACT
Hypertension is one of the very serious diseases and, recently, hypertensive patient longevity has been increased significantly. Therefore, the development of new antihypertensive drugs or bioactive compounds is very important to remedy or prevent hypertension. The antihypertensive angiotensin I-converting enzyme (ACE) inhibitor in water extracts from the brown-cultivar-fruiting-body of Hypsizygus marmoreus was purified with ultrafiltration, C18 solid phase extraction chromatography and reverse-phase HPLC, and the purified ACE inhibitor with inhibitory activity of IC50 value of 0.19 mg/mL was obtained. The purified ACE inhibitor was found to be a new oligopeptide with the sequence LSMGSASLSP. Its molecular weight was estimated to be 567.3 Da and the water extracts containing ACE inhibitor from Hypsizygus marmoreus showed a clear antihypertensive action a spontaneously hypertensive rat.

Show MeSH
Related in: MedlinePlus