書誌事項
- タイトル別名
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- Dynamics Study of Transmembrane Helix within Liposomes by Mass Spectrometry and Chemical Modification
- シツリョウ ブンセキ ト カガク シュウショク オ モチイタ マク カンツウ ヘリックス ノ マク ナイ ダイナミクス カイセキ
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抄録
We investigated the topology and dynamics of melittin within the liposomes using mass spectrometry combined with acetylation. According to matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and matrix-assisted laser desorption/ionization quadrupole ion trap time-of-flight mass spectrometry/mass spectrometry (MALDI-QIT-TOF MS/MS) analyses, melittin within the liposomes was mono acetylated; with the acetylated position being the N-terminal of melittin. This acetylation followed first-order kinetics. The rate constant was less than that of the acetylation of melittin in aqueous solution. Thus, it is suggested that the observed rate constant is that for the release of the N-terminal region of melittin to a water phase from the hydrophobic core of the liposomes. This approach has opened a new method in the study of dynamics of transmembrane helices within the membranes using mass spectrometry.
収録刊行物
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- 質量分析
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質量分析 58 (2), 75-79, 2010
一般社団法人 日本質量分析学会
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詳細情報 詳細情報について
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- CRID
- 1390001206496469248
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- NII論文ID
- 10026279044
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- NII書誌ID
- AN0010555X
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- ISSN
- 18804225
- 18843271
- 13408097
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- NDL書誌ID
- 10639515
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可