F枚rster resonance energy transfer between pyrene and bovine serum albumin: Effect of the hydrophobic pockets of cyclodextrins

详细信息	查看全文 | 推荐本文 |

• 作者：Arnab Maity^a ; Puspal Mukherjee^b ; Tarasankar Das^a ; Prasun Ghosh^a ; Pradipta Purkayastha^a ; ^{ppurkayastha@iiserkol.ac.in} ; ^{prad_purk@yahoo.com}
• 关键词：Resonance energy transfer ; Fluorescence ; Excimer ; Cyclodextrin ; Cavity size
• 刊名：Spectrochimica Acta Part A ; Molecular and Biomolecular Spectroscopy
• 出版年：2012
• 期刊代码：99_13861425
• 类别：ch
• 出版时间：15 June, 2012
• 卷：92
• 期：Complete
• 页码：382-387
• 文件大小：414 K

摘要

The phenomenon of F枚rster resonance energy transfer (FRET) between pyrene and bovine serum albumin (BSA) protein in presence of cyclodextrins (CDs) is explored in the present work. CDs provide hydrophobic environment and thus the aromatic molecules get encapsulated in them depending on the relative size and space. In this work we revealed that along with pyrene monomer, the side chains of amino acids in BSA can get trapped partly in the hydrophobic cavities of CDs if space permits. While being encapsulated by 尾-CD as pyrene monomer, it can interact with the BSA tryptophan moiety exposed toward the aqueous environment to form a dimer through 蟺-蟺 interaction. This, in turn, affects the energy transfer process by reducing the efficiency. On the other hand, pyrene excimer gets encapsulated in a 纬-CD molecule due to availability of enough space. The excimer shows a new band at a higher wavelength. This further reduces FRET efficiency due to scarcity of acceptor for the tryptophan moieties in BSA.