No abstract available.
Meningitis ; Peptidyl-Dipeptidase A

Background: Hypertension is a worldwide epidemic that has been recognized as the most leading global risk for mortality, with its prevalence associated with increased blood pressure, concomitant risks of cardiovascular and kidney diseases, and major commonality in individuals advanced in age. With the current treatment options for hypertension management, there is still a need to develop therapies that directly target receptors that aid in hypertension treatment. Methodology: The study focused on the in-silico profiling of the reported compounds from Areca catechu L. (fam. Arecaceae) towards the n-domain and c-domain angiotensin converting enzyme (ACE) receptor models. Bioisosteric replacement was used to create bioisosteres investigated for similar binding affinity. Results: Some A. catechu compounds exhibited favorable binding energies towards the n- and c-domain receptor models of ACE, binding in the same ACE ligand binding site as lisinopril, benazepril, and sampatrilat via similar interactions and amino acid residues. The majority of A. catechu compounds with favorable ACE binding energies belong to the phytochemical classes of flavonoids, polyphenols and phenolics, glycosides, and steroids. After in silico toxicity and pharmacokinetic profiling, the bioisosteres Leuco-DM02-39, Leuco-DM02-66, Leuco-DM05-60, Querc-DM09-63, and Querc-DM14-31 with binding energies higher than their parent compounds and comparable to lisinopril, benazepril, and sampatrilat were deemed the best. Conclusion A. catechu compounds have the potential to target ACE n-domain and c-domain receptor models. Three leucocyanidin and two quercetin bioisosteres exhibited favorable binding to the n-domain and c-domain ACE receptor models and could be further optimized to derive a promising antihypertensive agent through ACE inhibition.
Peptidyl-Dipeptidase A ; Areca ; Hypertension

No abstract available.
Angiotensins* ; Cough* ; Peptidyl-Dipeptidase A* ; Reflex*

We describe a patient with hyponatremia induced by the use of angiotensin-converting enzyme (ACE) inhibitor; imidapril HCl. Although the mechanism of severe hyponatremia due to ACE inhibitor is not clear, it is conceivable that ACE inhibitor therapy may complicate the syndrome of inappropriate secretion of antidiuretic hormone and induce hyponatremia. In addition, the possibility should be considered that hyponatremia in our patient is a presumptive interaction between oxcarbazepine and imidapril HCl.
Angiotensins* ; Humans ; Hyponatremia* ; Peptidyl-Dipeptidase A*

No abstract available.
Angiotensins* ; Diabetes Mellitus* ; Peptidyl-Dipeptidase A* ; Renal Insufficiency*

No abstract available.
Angiotensins* ; Humans ; Lung Neoplasms* ; Lung* ; Peptidyl-Dipeptidase A*

Blood Pressure ; physiology ; Humans ; Peptidyl-Dipeptidase A

Atrial Fibrillation ; pathology ; Humans ; Peptidyl-Dipeptidase A

No Abstract available.
Angiotensin-Converting Enzyme Inhibitors* ; Angiotensins* ; Peptidyl-Dipeptidase A*

Kluyveromyces fragilis KCTC 7260 and Saccharomyces cerevisiae KCTC 7904, which both grew well in pear marc extract, were selected and their growth profiles and physiological functionalities were determined. Both of the selected yeasts established maximal growth by 20 hr of cultivation at 30degrees C in pear marc extract. The cell-free extracts showed high antihypertensive angiotensin I-converting enzyme inhibitory activity of 68.9% and 52.1%, respectively. The extracts also displayed 9.2 U/mL and 12.0 U/mL of protease activity, respectively.
Kluyveromyces ; Peptidyl-Dipeptidase A ; Pyrus ; Saccharomyces cerevisiae ; Yeasts