Structural characterizations of protonated homodimers of amino acids:Revealed by infrared multiple photon dissociation(IRMPD) spectroscopy and theoretical calculations  

作　　者：Lifu Ma Juan Ren Ruxia Feng Kailin Zhang Xianglei Kong 

机构地区：[1]School of Precision Instrument and Opto-Electronics Engineering, Tianjin University [2]State Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Nankai University [3]Collaborative Innovation Center of Chemical Science and Engineering, Nankai University

出　　处：《Chinese Chemical Letters》2018年第9期1333-1339,共7页中国化学快报（英文版）

基　　金：supported by the National Natural Science Foundation of China(Nos.21475065,21627801 and 11704280)

摘　　要：Infrared multiple photon dissociation （IRMPD） spectroscopic and theoretical studies of protonated homodimers of amino acids generated by electrospray ionization in the gas phase have been reviewed. Results show that proton affinity （PA） may be applied as a probe to predict their structural type： salt- bridged or charge-solvated. Proline can be viewed as a reference. For an amino acid with a PA value higher than that of proline, the most stable conformation of its protonated homodimer tends to prefer salt- bridged conformation; otherwise, charge-solvated conformation is expected to be the most stable. However, side chain effects may cause the inaccuracy in structural determination due to the strong interactions with the charge, which makes the charge-solvated structure more stable even for species with high PA values. Temperature effect on distribution of different isomers is also very important. In lots of cases, the coexistence of multiple isomers is general, which makes the explanation of an overall IRMPD spectrum difficult. So a statistical view on the distribution of optimized isomers is very helpful.Infrared multiple photon dissociation （IRMPD） spectroscopic and theoretical studies of protonated homodimers of amino acids generated by electrospray ionization in the gas phase have been reviewed. Results show that proton affinity （PA） may be applied as a probe to predict their structural type： salt- bridged or charge-solvated. Proline can be viewed as a reference. For an amino acid with a PA value higher than that of proline, the most stable conformation of its protonated homodimer tends to prefer salt- bridged conformation; otherwise, charge-solvated conformation is expected to be the most stable. However, side chain effects may cause the inaccuracy in structural determination due to the strong interactions with the charge, which makes the charge-solvated structure more stable even for species with high PA values. Temperature effect on distribution of different isomers is also very important. In lots of cases, the coexistence of multiple isomers is general, which makes the explanation of an overall IRMPD spectrum difficult. So a statistical view on the distribution of optimized isomers is very helpful.

关 键 词：Amino acid HOMODIMER IRMPD spectroscopy Proton affinity Charge-solvated Salt-bridged ESI mass spectrometry 

分 类 号：O636[理学—高分子化学]