급성심근경색 진단을 위한 마이오글로빈 특이 펩타이드 기반 전기화학적 센서

Abstract

Acute myocardial infarction (AMI) is the major cause of death among adults worldwide. Occuring the AMI, biomakers are released into the blood circulation. Among them, myoglobin is the earliest biomarker of AMI. Herein, we developed an electorochemical biosensor based on myoglobin-specific peptides for the quantitative detection of myoglobin. The peptide, which specifically binds to myoglobin, was covalently immobilized on gold electrode functionalized with dithiobis(succinimidyl propionate) (DSP) self-assembled monolayer (SAM). The immobilization of the DSP and peptide was characterized with fluorescence microscopy and cyclic voltammetry (CV). The electrochemical performance of the biosensor with myoglobin was confirmed by CV and differential pulse voltammetry using Fe(CN)63-/4-as a redox probe. We successfully detected in a broad working range at 1 to 100 nM of myoglobin with limit of detection (LOD), 0.55 nM. Heme proteins such as hemoglobin and cytochrome C and myoglobin free serum were used to test the specificity of the biosensor to myoglobin.|전세계 성인의 주요 사망원인으로 급성심근경색을 들 수 가 있다. 급성심근경색이 발병하면 바이오마커가 혈중으로 방출된다. 이러한 급성심근경색의 바이오마커 중 마이오글로빈은 그 발현이 가장 빠르다. 우리는 이런 마이오글로빈의 검출을 위해 마이오글로빈 특이 펩타이드를 이용한 전기화학적 바이오 센서를 제작하였다. 마이오글로빈과 특이적으로 결합하는 펩타이드는 골드전극위에 형성된 DSP self-assembled monolayer에 공유결합으로 고정화되었다. 고정화된 DSP와 펩타이드는 형광과 CV를 통하여 확인하였다. 마이오글로빈과 바이오센서의 전기화학적 분석은 Fe(CN)63-/4-의 산화/환원반응 이용해 CV와 DPV를 사용하여 분석하였다. 1~100 nM의 넓은 범위의 마이오글로빈을 성공적으로 검출 할 수 있었으며, 0.55의 검출한계 값을 얻을 수 있었다. 헤모글로빈과 사이토크롬 C와 같은 헴 단백질과 마이오글로빈을 제거한 인간 혈청을 이용하여 펩타이드의 특이성을 확인하였다.; Acute myocardial infarction (AMI) is the major cause of death among adults worldwide. Occuring the AMI, biomakers are released into the blood circulation. Among them, myoglobin is the earliest biomarker of AMI. Herein, we developed an electorochemical biosensor based on myoglobin-specific peptides for the quantitative detection of myoglobin. The peptide, which specifically binds to myoglobin, was covalently immobilized on gold electrode functionalized with dithiobis(succinimidyl propionate) (DSP) self-assembled monolayer (SAM). The immobilization of the DSP and peptide was characterized with fluorescence microscopy and cyclic voltammetry (CV). The electrochemical performance of the biosensor with myoglobin was confirmed by CV and differential pulse voltammetry using Fe(CN)63-/4-as a redox probe. We successfully detected in a broad working range at 1 to 100 nM of myoglobin with limit of detection (LOD), 0.55 nM. Heme proteins such as hemoglobin and cytochrome C and myoglobin free serum were used to test the specificity of the biosensor to myoglobin.