Porphyrin light-harvesting arrays constructed in the recombinant tobacco mosaic virus scaffold.

نویسندگان

  • Masayuki Endo
  • Mamoru Fujitsuka
  • Tetsuro Majima
چکیده

We have demonstrated the construction of multiple porphyrin arrays in the tobacco mosaic virus (TMV) supramolecular structures by self-assembly of recombinant TMV coat protein (TMVCP) monomers, in which Zn-coordinated porphyrin (ZnP) and free-base porphyrin (FbP) were site-selectively incorporated. The photophysical properties of porphyrin moieties incorporated in the TMV assemblies were also characterized. TMV-porphyrin conjugates employed as building blocks self-assembled into unique disk and rod structures under the proper conditions as similar to native TMV assemblies. The mixture of a ZnP donor and an FbP acceptor was packed in the TMV assembly and showed energy transfer and light-harvesting activity. The detailed photophysical properties of the arrayed porphyrins in the TMV assemblies were examined by time-resolved fluorescence spectroscopy, and the energy transfer rates were determined to be 3.1-6.4x10(9) s(-1). The results indicate that the porphyrins are placed at the expected positions in the TMV assemblies.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Study on Genetic Diversity of Terminal Fragment Sequence of Isolated Persian Tobacco Mosaic Virus

Tobacco mosaic virus (TMV) is one of the devastating plant viruses in the world that infects more than 200 plant species. Movement protein plays a supportive role in the movement of other plant viruses, and viral coat protein is highly expressed in infected plants and affects replication and movements of TMV. In order to investigate genetic variation in the terminal fragment sequence in Iranian...

متن کامل

High-efficiency protein expression in plants from agroinfection-compatible Tobacco mosaic virus expression vectors

BACKGROUND Plants are increasingly being examined as alternative recombinant protein expression systems. Recombinant protein expression levels in plants from Tobacco mosaic virus (TMV)-based vectors are much higher than those possible from plant promoters. However the common TMV expression vectors are costly, and at times technically challenging, to work with. Therefore it was a goal to develop...

متن کامل

Tomato and Tobacco Phytoene Desaturase Gene Silencing by Virus-Induced Gene Silencing (VIGS) Technique

Background and Aims: Virus-Induced Gene Silencing (VIGS) is a virus vector technology that exploits antiviral defense mechanism. By infecting plants with recombinant viruses containing host genes inserted in the viral genome, VIGS achieves the RNA silencing process. The purpose of this study was to investigate the possibility of tomato (Lycopersicon esculentum Mill.) and tobacco (Nicotiana be...

متن کامل

Fabrication and characterization of gold nano-wires templated on virus-like arrays of tobacco mosaic virus coat proteins

The rod-shaped plant virus tobacco mosaic virus (TMV) is widely used as a nano-fabrication template, and chimeric peptide expression on its major coat protein has extended its potential applications. Here we describe a simple bacterial expression system for production and rapid purification of recombinant chimeric TMV coat protein carrying C-terminal peptide tags. These proteins do not bind TMV...

متن کامل

Expression of Recombinant Porcine Preprorelaxin in Nicotiana Tabacum

Relaxin is a small peptide hormone that has demonstrated potential therapeutic actions for cardiovascular disease and fibrosis. Additionally, relaxin has demonstrated the ability to protect the heart from injuries caused by ischemia and reperfusion, promote the healing of ischemic ulcers, and counteract allergic responses. The objective of this research was to express fully processed porcine re...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Chemistry

دوره 13 31  شماره 

صفحات  -

تاریخ انتشار 2007