摘要
通过抗菌肽Ａ与抗菌肽Ｂ两种分子的粉末固体状态、水溶液状态空间构象的喇曼光谱分析，表明这两种抗菌肽具有不同的主链构象，在固态中分别以无规卷曲、α螺旋为主，在水溶液中分别以α螺旋、β结构为主．两种分子在水溶液中Ｃ－Ｓ侧链构象分别为扭式与反式．但色氨酸侧链环境分析表明，两种分子在水溶液中均为色氨酸残基处于部分或完全暴露状态。
The laser raman spectra of both Cecropin A and Cecropin B in lyophilized powders state and aqueous solution state respectively have been obtained.main chain spatial conformational difference between two type Cecropin have been studied by raman analysis method.in powders state,dominant structure of Cecropin A and B are random coil and α-helix,respectively.in solution state,that are α-helix and β-structure,respectively.the C-S side chain conformation of methionine are gauche and trans type,respectively.the side chain microenvironment of Trp residue is partly“exposed”or all “exposed”state.the conclusion provides an evidence directly for Trp residue possess the primary anchor function that cause whole molecule close contact to the cell membrane.
出处
《南京师大学报（自然科学版）》
CAS
CSCD
1998年第4期58-63,共6页
Journal of Nanjing Normal University(Natural Science Edition)
基金
国家自然科学基金
关键词
抗菌肽A
抗菌肽B
空间构象
激光喇曼光谱
Cecropin A,Cecropin B,Spatial conformation,Laser Raman Spectroscopy
