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| Type |
Oral Presentation |
| Area |
Oral Presentation of Young Analytical Chemists Ⅱ |
| Room No. |
303호 |
| Time |
FRI 10:26-: |
| Code |
ANAL2.O-40 |
| Subject |
MALDI-TOF/TOF applications of TEMPO-assisted free radical initiated peptide sequencing (FRIPS) mass spectrometry |
| Authors |
송인수, 차상원1, 오한빈*
서강대학교 화학과, Korea
1한국외국어대학교 화학과, Korea
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| Abstract |
Unlike CID-based peptide sequencing, TEMPO-assisted FRIPS makes use of a radical species for peptide sequencing. In this method, a peptide is conjugated with o-TEMPO-Bz-C(O)-NHS and thus generating o-TEMPO-Bz-C(O)-peptides. When o-TEMPO-Bz-C(O)-peptides is subjected to collisional activation, o-TEMPO-Bz-C(O)-peptides undergoes homolytic cleavage, forming ∙Bz-C(O)-peptide. Then∙Bz-C(O)-peptide produces a, c, x, and z-type products upon the secondary collisional activation. So far, ESI has been used for the TEMPO-assisted FRIPS MS. In this study, MALDI-TOF/TOF was performed on o-TEMPO-Bz-C(O)-peptides. It was revealed that MALDI ionization for o-TEMPO-Bz-C(O)-peptides was greatly affected by the matrix. 3-HPA(3-Hydroxypicolinic acid) was found to be a good matrix, whereas DHB, CHCA, showed a very low ionization efficiency. MALDI MS/MS of the detected o-TEMPO-Bz-C(O)-peptides yielded a, c, x and z-type products. |
| E-mail |
insu6122@naver.com |
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119th General Meeting of the KCS