化学
直链淀粉
螺旋(腹足类)
分子
结晶学
核磁共振波谱
光谱学
包合物
红外光谱学
立体化学
有机化学
淀粉
物理
蜗牛
生物
量子力学
生态学
作者
Yuichi Tozuka,Aya Takeshita,Ayako Nagae,Arpansiree Wongmekiat,Kunikazu Moribe,Toshio Oguchi,Keiji Yamamoto
出处
期刊:Chemical & Pharmaceutical Bulletin
[Pharmaceutical Society of Japan]
日期:2006-01-01
卷期号:54 (8): 1097-1101
被引量:34
摘要
The inclusion compound formation between linear amylose of molecular weight 102500 (AS100) and p-aminobenzoic acid (PA) during the sealed-heating process was investigated by powder X-ray diffractometry, infrared spectroscopy and solid state NMR spectroscopy. Sealed-heating of AS100 and PA at 100 degrees C for 6 h provided an inclusion compound with 6(1)-helix structure, while a 7(1)-helix structure was found when sealed-heating was carried out at 150 degrees C for 1 h. The formation of an inclusion compound was not observed when sealed-heating was performed at 50 degrees C for 6 h. The 7(1)-helix inclusion compound maintained its structure even during storage at high temperature while the 6(1)-helix inclusion compound decomposed and returned to the original V(a)-amylose upon heating to 180 degrees C. Quantitative determination revealed that one PA molecule could be included per one helical turn of AS100 for both 6(1)-helix and 7(1)-helix inclusion compounds. Solid state NMR spectroscopy suggested that PA molecules were included in the amylose helix core in the 7(1)-helix inclusion compound, while in the case of 6(1)-helix inclusion compound, PA molecules were accommodated in the interstices between amylose helices. Moreover, the inclusion compound formation by sealed-heating of AS100 was also observed when using PA analogues as guest compounds. The binding ratio of AS100 and PA analogues varied depending on the size of guest molecules.
科研通智能强力驱动
Strongly Powered by AbleSci AI