短杆菌肽A在十六烷基三甲基溴化铵胶束介质中的构象。
Conformation of gramicidin-A in CTAB micellar media.
作者信息
Shobini J, Mishra A K, Chandra Nagasuma
机构信息
Department of Chemistry, Indian Institute of Technology--Madras, Chennai 600 036, India.
出版信息
J Photochem Photobiol B. 2003 May-Jun;70(2):117-24. doi: 10.1016/s1011-1344(03)00055-1.
Gramicidin A (gA) is a linear pentadecapeptide, which exhibits various conformations depending on the environment. The conformational behavior of gA in spherical and rod-shaped cationic micelles formed by cetyltrimethylammonium bromide (CTAB) surfactant has been studied using circular dichroism (CD) and fluorescence spectroscopy, and a probable structure of gramicidin A in CTAB media has been proposed. A CD study shows that gramicidin A assumes beta(6.3) helical structure in cationic spherical as well as rod-shaped CTAB micellar media. Modeling studies show the flexibility of the side chain conformation particularly in tryptophan-9. Study of intrinsic fluorescence of tryptophans in gramicidin A indicates three distinct environments for the four-tryptophan residues in CTAB media.
短杆菌肽A（gA）是一种线性十五肽，其构象会因环境而异。利用圆二色光谱（CD）和荧光光谱研究了短杆菌肽A在由十六烷基三甲基溴化铵（CTAB）表面活性剂形成的球形和棒状阳离子胶束中的构象行为，并提出了短杆菌肽A在CTAB介质中的可能结构。一项CD研究表明，短杆菌肽A在阳离子球形以及棒状CTAB胶束介质中呈现β(6.3)螺旋结构。建模研究表明侧链构象具有灵活性，尤其是色氨酸-9处。对短杆菌肽A中色氨酸的固有荧光研究表明，在CTAB介质中四个色氨酸残基存在三种不同的环境。
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