TY - JOUR
T1 - Effects of Matrices and Additives on Multiple Charge Formation of Proteins in MALDI–MS Analysis
AU - Choi, Hyemin
AU - Lee, Dabin
AU - Kim, Yeoseon
AU - Nguyen, Huu Quang
AU - Han, Sol
AU - Kim, Jeongkwon
N1 - Funding Information:
This research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (2016R1D1A1B02008854) and supported by the Korea Basic Science Institute (KBSI) under the R&D program (Project No. D38621) supervised by the Ministry of Science and ICT.
Publisher Copyright:
© 2019, American Society for Mass Spectrometry.
PY - 2019/7/15
Y1 - 2019/7/15
N2 - The sinapinic acid (SA) matrix has frequently been used for protein analysis in matrix-assisted laser desorption/ionization–mass spectrometry (MALDI–MS). However, the SA matrix does not result in the formation of distinctive multiple protein charge states, whereas the 2-nitrophloroglucinol (2-NPG) matrix is capable of this. The formation of multiple charge states in the MALDI–MS analysis of proteins is advantageous in that it results in higher accuracy. In this study, the mass spectra of several common standard proteins, namely cytochrome c, myoglobin, bovine serum albumin (BSA), and immunoglobulin G (IgG), were compared using various matrices (2,5-dihydroxybenzoic acid, α-cyano-hydroxycinnamic acid, SA, and 2-NPG). Furthermore, the mass spectra of two large standard proteins (BSA and IgG) using various acid additives (H3PO4, HNO3, H2SO4, HCl, and trifluoroacetic acid) with the 2-NPG matrix were also compared. Among the different matrices, 2-NPG provided the broadest range of multiple protein charge states, while, among the different additives, the 2-NPG matrix in combination with HCl generated the broadest multiple charge states as well as the most intense protein peaks.
AB - The sinapinic acid (SA) matrix has frequently been used for protein analysis in matrix-assisted laser desorption/ionization–mass spectrometry (MALDI–MS). However, the SA matrix does not result in the formation of distinctive multiple protein charge states, whereas the 2-nitrophloroglucinol (2-NPG) matrix is capable of this. The formation of multiple charge states in the MALDI–MS analysis of proteins is advantageous in that it results in higher accuracy. In this study, the mass spectra of several common standard proteins, namely cytochrome c, myoglobin, bovine serum albumin (BSA), and immunoglobulin G (IgG), were compared using various matrices (2,5-dihydroxybenzoic acid, α-cyano-hydroxycinnamic acid, SA, and 2-NPG). Furthermore, the mass spectra of two large standard proteins (BSA and IgG) using various acid additives (H3PO4, HNO3, H2SO4, HCl, and trifluoroacetic acid) with the 2-NPG matrix were also compared. Among the different matrices, 2-NPG provided the broadest range of multiple protein charge states, while, among the different additives, the 2-NPG matrix in combination with HCl generated the broadest multiple charge states as well as the most intense protein peaks.
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U2 - 10.1007/s13361-019-02213-7
DO - 10.1007/s13361-019-02213-7
M3 - Article
C2 - 31044356
AN - SCOPUS:85065313825
SN - 1044-0305
VL - 30
SP - 1174
EP - 1178
JO - Journal of the American Society for Mass Spectrometry
JF - Journal of the American Society for Mass Spectrometry
IS - 7
ER -