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학술발표회초록보기

초록문의 abstract@kcsnet.or.kr

결제문의 member@kcsnet.or.kr

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  • 09월 04일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제114회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Free radical initiated peptide sequencing (FRIPS) studies for phosphorylated peptides

등록일
2014년 8월 25일 15시 40분 34초
접수번호
0182
발표코드
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발표시간
10월 15일 (수요일) 16:00~19:00
발표형식
포스터
발표분야
분석화학
저자 및
공동저자
오한빈
서강대학교 화학과, Korea
Post-translational modifications (PTMs), particularly, phosphorylations, are the important step that plays an important role in biological system in vivo. Phosphorylation PTMs are involved in cell death, cell-cell signaling, and various biological processes. Due to its importance, extensive investigations have been made towards the development of phosphorylation PTM analysis. On the other way, our group has development a new radical-based peptide backbone dissociation method, the so-called, ‘free radical initiated peptide sequencing (FRIPS)’. In this method, a TEMPO-containing radical initiator is conjugated to the N-terminus or lysine side chain. Upon collisional activation, a benzylic radical can be generated and this radical species can initiate peptide backbone dissociations upon the secondary application of collisional activation. In this study, we have explored the opportunity of using FRIPS for the analysis of phosphorylated peptides. We have examined the peptides phosphorylated at serine or tyrosine site. For the phosphopeptides modified at tyrosine, it was found that the phosphor-ether bond could survive even at the collisional activation with which the benzylic radical was generated. As a result, the phosphorylation site could be determined in FRIPS MS experiments. In the case of peptides with a phosphoserine residue, dephosphorylation was found to occur extensively. The detailed results will be presented in the symposium.

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