Short Synthetic Peptides as Inhibitors of Angiotensin Converting Enzyme.

The ectoenzyme - angiotensin I converting enzyme (ACE) is widespread in human body [1]. It is well known for his pivotal role in blood pressure regulation and renal and cardiovascular function. ACE is capable of cleaving wide range of substrates and affects many other physiologic processes in addition to blood pressure control. These include hematopoiesis, reproduction, renal development, renal function, and the immune response. The inhibitors of Angiotensin I converting enzyme (ACE) are first line of therapy for hypertension, heart failure, myocardial infarction and diabetic nephropathy. Several potent synthetic ACE inhibitors such a captopril, lisinopril, enalapril, ect. have been used in the clinical practice for treatment of hypertension and heart failure. However synthetic ACE inhibitors can have side effects such dry cough, skin rashes, toxicity, impaired renal function, hyperkalaemia etc., as well as low oral bioavailability. ACE inhibitors isolated from different natural sources can effectively control blood pressure and in the same time they have minimal side effects. In recent years there is an increasing interest in isolation of bioactive peptides with antihypertensive action during enzyme hydrolysis of food with different origin – milk protein, egg protein, different cheeses, white and red wine, vegetable proteins and marine sources [2, 3]. Therefore the quantity of these peptides in natural sources is quite low and other strategies for obtaining them are required. The aim of this study was to design and synthesize small natural biologically active peptides as specific ACE inhibitors and determining their biological properties.