| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2003: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 2002: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2001: ¥1,400,000 (Direct Cost: ¥1,400,000)
|
|---|
| Research Abstract |
The goal of this project focuses on the purification and the utilization of potential bioactive peptides in human protein sequences. For example, angiotensin I-converting enzyme (ACE) inhibitory peptides derived from an enzymatic hydrolysate of human proteins are hopeful for the anti-hypertensive medicines. Another goal is that the retro-inverso peptides, which consist of all D-amino acids and peptides containing reversed bonds, are synthesized and studied for the seeds of novel peptidyl medicines.
The results of this project are as follows ;
1. Purification and characterization of novel ACE inhibitory peptides.
(1)Two novel ACE inhibitory peptides were purified from a papaic hydrolysate of human gamma globulin. The 1C50 values of this peptides, VAW and VSW, were found 4.3 p mol/L and 13 p molIL, respectively, and both peptides showed the competitive inhibition.
(2)The two enzymatic activity of ACE, which converts angiotensin I to angiotensin II and degradates bradykinin, were measured independently with reversed-phase I-IPLC. AW and VAW among several active peptides found were found to be selective inhibitors that have more potent inhibitory activity against angiotensin I conversion than bradykinin degradation.
(3)The retro-inverso peptides, dWdAdV, dWdSdV and dYdIdL were synthesized and their ACE inhibitory activity were measured.
2. Purification of other potential bioactive peptides in human protein sequences.
The four novel cathepsin B inhibitory peptides were purified from a thermolytic hydrolysate of human plasma, and two more novel inhibitory peptides were from a tryptic and chyrnotryptic hydrolysate of human serum albumin.
|
