Human angiotensin I‐converting enzyme study by surface‐enhanced Raman spectroscopy

Angiotensin I‐converting enzyme (ACE) is a glycoprotein, consisting of two homologous domains within a single polypeptide chain. ACE concentration in biological fluids is an important parameter of clinical observation; its increase or decrease may accompany various pathologies. Currently, the exact crystal structure of the two‐domain ACE form is still unknown because of microheterogeneity and intensity of the enzyme glycosylation. Raman spectroscopy provides the qualitative and quantitative analysis of many compounds, including proteins. For the first time, surface‐enhanced Raman scattering (SERS) spectra of native and thermo‐denatured human ACE have been demonstrated with full assignment. Denaturation leads to SERS intensity increase and bands shifting. Detailed band assignment and discussion are included to elucidate the potential site of ACE interaction with the silver surface. Based on SERS spectra, we characterized the region on the ACE molecule in contact with the substrate and demonstrated the model of the two‐domain ACE adsorbed on a silver matrix. SERS spectra of native and thermo‐denatured human ACE have been demonstrated with the full assignment. Analysis of ACE spectra could be beneficial for the estimation of the enzyme content in different sources. Based on SERS spectra, we attempted to show a putative contact area model of two‐domain ACE adsorbed on the silver matrix.