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Human angiotensin I‐converting enzyme study by surface‐enhanced Raman spectroscopy
Author(s) -
Boginskaya Irina,
Nechaeva Natalia,
Tikhomirova Victoria,
Kryukova Olga,
Evdokimov Valery,
Bulaeva Naida,
Golukhova Elena,
Ryzhikov Ilya,
Kost Olga,
Afanasev Konstantin,
Vereshchagin Konstantin,
Kurochkin Ilya
Publication year - 2021
Publication title -
journal of raman spectroscopy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.748
H-Index - 110
eISSN - 1097-4555
pISSN - 0377-0486
DOI - 10.1002/jrs.6068
Subject(s) - raman spectroscopy , raman scattering , chemistry , denaturation (fissile materials) , substrate (aquarium) , glycoprotein , angiotensin converting enzyme , surface enhanced raman spectroscopy , enzyme , molecule , crystallography , analytical chemistry (journal) , biochemistry , nuclear chemistry , chromatography , organic chemistry , biology , ecology , physics , blood pressure , optics , endocrinology
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.