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  • 09월 08일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제116회 대한화학회 학술발표회, 총회 및 기기전시회 안내 C-terminal Modification with Putrescine for Relative Quantification by LC-MS

2015년 9월 3일 15시 37분 26초
ANAL2.O-15 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
금 15시 : 34분
분석화학 - Oral Presentation of Young Analytical Chemists II
저자 및
김상진, 임재민*
창원대학교 화학과, Korea
Proteins are associated with many diseases such as cancer and diabetes. Recently protein quantitative analysis was diagnosed biomarker of many diseases by mass spectrometry. Protein quantification by mass spectrometry was generally used the isotope labeling. The use of typical isotope tags have developed in vivo or in vitro labeling techniques like the stable isotope labeling by amino acids in cell culture (SILAC), Isotope-coded affinity tag (ICAT) and H2O18 protease technique. In this study, we have developed carboxyl modification of peptides as a method for quantitative analysis using normal putrescine (1,4-butanediamine) and heavy putrescine (1,4-butane-d8-diamine) by mass spectrometry. The carboxyl-reactive amidation reagent 1-[Bis(dimethylamino)methylene]-1H-1,2,3-triazolo[4,5-b]pyridinium 3-oxid hexafluorophosphate (HATU) is used to amidate the carboxylic acid group of the peptide angiotensin II and the tryptic digested albumin peptides to normal putrescine and heavy putrescine. As a result, amidation reaction using HATU with heavy putrescine as labeling shows 8 Da difference in comparison with original peptide which can overcome the isotope distribution overlapping. In addition, the carboxyl modified peptides increased the most abundant charge state compared to native peptides to enhanced fragmentation for electron-transfer dissociation (ETD).