Investigation of Calmodulin-Peptide Interactions Using Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry


Autoria(s): Wang ZF; Yu XM; Cui M; Liu ZQ; Song FR; Liu SY
Data(s)

2009

Resumo

In this report, matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) was used to study the binding interactions between calmodulin and two target peptides (melittin and substance P). Various matrix conditions were tested and the less acidic matrix DHAP and THAP were found to favor the survival of the intact calcium-calmodulin as well as the calmodulin-peptide complexes. However, the application of direct MALDI-MS to detect the intact complexes turned out to be very difficult due to the dissociation of the complexes and the formation of nonspecific aggregates. In contrast, the specific binding of the target peptides to calmodulin could be easily deduced using intensity-fading (IF) MALDI-MS. Compared with the nonbinding control, clear reduction in the ion abundances of the target peptides was observed with the addition of calmodulin.

Identificador

http://202.98.16.49/handle/322003/11495

http://www.irgrid.ac.cn/handle/1471x/147986

Idioma(s)

英语

Fonte

Wang ZF;Yu XM;Cui M;Liu ZQ;Song FR;Liu SY.Investigation of Calmodulin-Peptide Interactions Using Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry,JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY ,2009,20(4):576-583

Palavras-Chave #ION-CYCLOTRON RESONANCE #MALDI-TOF-MS #ELECTROSPRAY-IONIZATION #NONCOVALENT COMPLEXES #PROTEASE INHIBITORS #BIOLOGICAL SAMPLES #MELITTIN COMPLEX #INFLUENZA-VIRUS #ESI-MS #BINDING
Tipo

期刊论文