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Bz-Phe-Ala-Pro, also known as benzoyl-Phe-Ala-Pro or BPAP, is a synthetic substrate for angiotensin-converting enzyme (ACE). The benzoylated tripeptide has been used in biochemical and vascular research to measure ACE-dependent hydrolysis without introducing the direct vasoactive effects associated with endogenous angiotensin peptides.
Its defined structure makes BPAP useful for enzyme kinetics, ACE inhibition studies and evaluation of endothelial ACE activity.
Product Information
| Property | Specification |
|---|---|
| Product Name | Bz-Phe-Ala-Pro |
| Catalog No. | AS2613 |
| CAS No. | 69677-91-4 |
| Sequence | Bz-Phe-Ala-Pro |
| Molecular Formula | C24H27N3O5 |
| Molecular Weight | Approximately 437.49 Da |
| Enzyme Target | Angiotensin-converting enzyme (ACE) |
| Peptide Class | Synthetic ACE substrate |
| Research Areas | ACE activity, enzyme kinetics, endothelial biology, inhibitor studies |
| Purity | Crude to 98% |
ACE-Dependent Hydrolysis
ACE is a zinc-dependent dipeptidyl carboxypeptidase involved in processing several vasoactive peptides. Bz-Phe-Ala-Pro provides a compact synthetic substrate for examining its catalytic activity under controlled experimental conditions.
Classical studies demonstrated ACE-dependent hydrolysis of BPAP in cultured vascular endothelial cells, pulmonary vascular systems and coronary circulation. ACE inhibitors and metal-chelating conditions markedly reduce substrate turnover, supporting its use as an enzymatic probe.
We consider the distinction between BPAP and native angiotensin I important for experimental planning. BPAP is a synthetic ACE substrate with its own cleavage chemistry and should be identified by its molecular structure when kinetic data are compared.
Endothelial ACE Research
Radiolabeled BPAP has historically been used to examine endothelium-bound ACE activity during passage through pulmonary and coronary vascular beds.
This application reflects a useful property of the molecule: enzyme-dependent substrate conversion can be studied independently of the receptor signaling produced by angiotensin II.
Experimental Considerations
ACE activity measurements are sensitive to substrate concentration, enzyme source, chloride concentration, pH and metal-ion conditions. Quantitative studies should therefore use consistent reaction conditions and appropriate inhibitor controls.
Our Peptide Quality Control capabilities support analytical HPLC and mass spectrometry according to the selected product specification.
Frequently Asked Questions
Is Bz-Phe-Ala-Pro the same peptide as angiotensin I?
No. Bz-Phe-Ala-Pro is a synthetic tripeptide ACE substrate. Human angiotensin I is a 10-residue endogenous peptide with the sequence DRVYIHPFHL.
What can Bz-Phe-Ala-Pro be used to measure?
It can be used in assays investigating ACE catalytic activity, enzyme inhibition and endothelium-associated ACE function.
Can alternative ACE substrates be synthesized?
Alternative peptide sequences, labeled substrates and assay-oriented designs can be evaluated through Chemical Peptide Synthesis.