Angiotensin converting enzyme inhibitors: N-Substituted monocyclic and bicyclic amino acid derivatives

1983 ◽  
Vol 26 (9) ◽  
pp. 1267-1277 ◽  
Author(s):  
James L. Stanton ◽  
Norbert Gruenfeld ◽  
Joseph E. Babiarz ◽  
Michael H. Ackerman ◽  
Robert C. Friedmann ◽  
...  
Keyword(s):  
Amino Acid ◽  
Angiotensin Converting Enzyme ◽  
Enzyme Inhibitors ◽  
Angiotensin Converting Enzyme Inhibitors ◽  
Amino Acid Derivatives ◽  
Converting Enzyme ◽  
Converting Enzyme Inhibitors

Synthesis and Activity Determination of Angiotensin Converting Enzyme Inhibitors Derived from αs1-Casein Protein

2011 ◽  
Vol 365 ◽  
pp. 180-186
Author(s):  
Ya Lin Ren ◽  
Yan Jun Cong ◽  
Cun She Chen
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Angiotensin Converting Enzyme ◽  
Enzyme Inhibitors ◽  
Solid Phase ◽  
Angiotensin Converting Enzyme Inhibitors ◽  
Converting Enzyme ◽  
Converting Enzyme Inhibitors ◽  
High Biological Activity ◽  
Casein Protein

A lot of peptides were synthesized on the basis of the sequence of αs1-casein. These tri-peptides with the characteristics of low toxicity and high biological activity will be applied to screen a new type of antihypertensive drug. Angiotensin-converting enzyme inhibitors (ACEI) with the better biological activity were screened and their structure-activity relationship was studied. The method of Fmoc solid-phase synthesis had been used to synthesize tri-peptides, and the principle, species, steps of which had been introduced respectively. HPLC assay was applied to screen the activity of ACEI by detecting the concentrate of hippuric acid, which can correspond with the inhibitory activity of tri-peptides. The results showed that the tri-peptides containing hydrophobic amino acid or praline had higher inhibition activity, and the same to the one that containing an aromatic amino acid in N-terminal.

Synthesis and Activity Determination of Angiotensin Converting Enzyme Inhibitors Derived from αs1-Casein Protein

2010 ◽  
Vol 43 ◽  
pp. 253-256
Author(s):  
Ming Yu Huang ◽  
Jing Jing Lv ◽  
Hong Jun Ni ◽  
Yu Zhu ◽  
Fu Bao Zhang
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Angiotensin Converting Enzyme ◽  
Enzyme Inhibitors ◽  
Solid Phase ◽  
Angiotensin Converting Enzyme Inhibitors ◽  
Converting Enzyme ◽  
Converting Enzyme Inhibitors ◽  
High Biological Activity ◽  
Casein Protein

A lot of peptides were synthesized on the basis of the sequence of αs1-casein. These tri-peptides with the characteristics of low toxicity and high biological activity will be applied to screen a new type of antihypertensive drug. Angiotensin-converting enzyme inhibitors (ACEI) with the better biological activity were screened and their structure-activity relationship was studied. The method of Fmoc solid-phase synthesis had been used to synthesize tri-peptides, and the principle, species, steps of which had been introduced respectively. HPLC assay was applied to screen the activity of ACEI by detecting the concentrate of hippuric acid, which can correspond with the inhibitory activity of tri-peptides. The results showed that the tri-peptides containing hydrophobic amino acid or praline had higher inhibition activity, and the same to the one that containing an aromatic amino acid in N-terminal.

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