物理化学学报
物理化學學報
물이화학학보
ACTA PHYSICO-CHIMICA SINICA
2008年
9期
1558-1562
,共5页
芋螺马芬%芋螺肽%D-苯丙氨酸%NMR溶液结构%pH敏感
芋螺馬芬%芋螺肽%D-苯丙氨痠%NMR溶液結構%pH敏感
우라마분%우라태%D-분병안산%NMR용액결구%pH민감
Conomarphin%Conopeptide%D-Phenylalanine%NMR solution structure%pH sensitive
从大理石芋螺毒液中分离得到一种新型的含有D型氨基酸,并属于M超家族的芋螺毒素--芋螺马芬.应用2D NMR方法测定了芋螺马芬在pH 5条件下的三维结构,由205个距离约束,8个二面角约束以及两个氢键约束得到了20个最优结构.它们骨架原子的均方根偏差为(0.074±0.029)nm.芋螺马芬在pH 5条件下的二级结构是位于C端的一个短的310螺旋,同时在Ala6附近呈一个较为松散的环状区域.将芋螺马芬在pH 5以及pH 3条件下的溶液结构以及表面电荷进行了比较.尽管芋螺马芬在pH 5条件下的溶液结构与在pH 3条件下的相比,在C端有一个相似的二级结构单元,但是整体的骨架结构截然不同,在pH 5条件下,芋螺马芬的表面结构从正面看起来像一个"曲臂".结构的差异揭示了芋螺马芬对pH相当敏感,预示着它在体内的活性可能与酸度密切相关.
從大理石芋螺毒液中分離得到一種新型的含有D型氨基痠,併屬于M超傢族的芋螺毒素--芋螺馬芬.應用2D NMR方法測定瞭芋螺馬芬在pH 5條件下的三維結構,由205箇距離約束,8箇二麵角約束以及兩箇氫鍵約束得到瞭20箇最優結構.它們骨架原子的均方根偏差為(0.074±0.029)nm.芋螺馬芬在pH 5條件下的二級結構是位于C耑的一箇短的310螺鏇,同時在Ala6附近呈一箇較為鬆散的環狀區域.將芋螺馬芬在pH 5以及pH 3條件下的溶液結構以及錶麵電荷進行瞭比較.儘管芋螺馬芬在pH 5條件下的溶液結構與在pH 3條件下的相比,在C耑有一箇相似的二級結構單元,但是整體的骨架結構截然不同,在pH 5條件下,芋螺馬芬的錶麵結構從正麵看起來像一箇"麯臂".結構的差異揭示瞭芋螺馬芬對pH相噹敏感,預示著它在體內的活性可能與痠度密切相關.
종대리석우라독액중분리득도일충신형적함유D형안기산,병속우M초가족적우라독소--우라마분.응용2D NMR방법측정료우라마분재pH 5조건하적삼유결구,유205개거리약속,8개이면각약속이급량개경건약속득도료20개최우결구.타문골가원자적균방근편차위(0.074±0.029)nm.우라마분재pH 5조건하적이급결구시위우C단적일개단적310라선,동시재Ala6부근정일개교위송산적배상구역.장우라마분재pH 5이급pH 3조건하적용액결구이급표면전하진행료비교.진관우라마분재pH 5조건하적용액결구여재pH 3조건하적상비,재C단유일개상사적이급결구단원,단시정체적골가결구절연불동,재pH 5조건하,우라마분적표면결구종정면간기래상일개"곡비".결구적차이게시료우라마분대pH상당민감,예시착타재체내적활성가능여산도밀절상관.
Conomarphin, a novel conopeptide containing D-amino acid, was identified from the venom of Conus marmoreus and classified into M-superfamily of conotoxin. In this article, we reported the 3D structure of conomarphin at pH 5 determined using 2D 1H NMR method in aqueous solution. Twenty converged structures of this peptide were obtained based on 205 distance constraints, 8 dihedral angle constraints, and 2 hydrogen bond constraints. The root mean square deviation (RMSD) values of the backbone atoms were (0.074±0.029) nm. The refined structure of conomarphin at pH 5 contained a short 310-helix at C-terminal of the peptide. It was also characterized by a loose loop centered at Ala6. Comparison of structural and electrostatic potential between conomarphin at pH 3 and pH 5 were presented. Although the solution structure of conomarphin at pH 5 shared part of the same secondary structure element with the structure of conomarphin at pH 3, it adopted a distinctive backbone conformation with the overall molecule resembling a "flexcual arm" when viewed from the front. Structural differences imply that this conopeptide is rather pH sensitive and its bioactivity in vivo might be related to the acidity.