Issue 18, 2011
From the journal:

Chemical Communications

A quantum-dot based protein module for in vivo monitoring of protease activity through fluorescence resonance energy transfer†

Payal Biswas,a   Lakshmi N. Cella,bc   Seung Hyun Kang,a   Ashok Mulchandani,a   Marylynn V. Yatesd  and  Wilfred Chen*b  

* Corresponding authors

a Department of Chemical and Environmental Engineering, University of California, Riverside, California 92521, USA

b Department of Chemical Engineering, University of Delaware, Newark, USA
E-mail: wilfred@udel.edu
Tel: +1 (302)-831-26327

c Cell Molecular & Developmental Biology Graduate Program, University of California, Riverside, California 92521, USA

d Department of Environmental Sciences, University of California, Riverside, California 92521, USA

Abstract

Here, we present a new generation of nanoscale probes for in vivo monitoring of protease activity by fluorescence resonance energy transfer (FRET). The approach is based on a genetically programmable protein module carrying a fluorescently labeled, protease-specific sequence that can self-assemble onto quantum dots. The protein module was used for real-time detection of human immunodeficiency virus type-1 protease (HIV-1 Pr) activity as well as quantitative assessment of inhibitor efficiency.

Graphical abstract: A quantum-dot based protein module for in vivo monitoring of protease activity through fluorescence resonance energy transfer

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/C1CC10648A
Article type
Communication
Submitted
01 Feb 2011
Accepted
11 Mar 2011
First published
29 Mar 2011

Chem. Commun., 2011,47, 5259-5261

Permissions

Request permissions

A quantum-dot based protein module for in vivo monitoring of protease activity through fluorescence resonance energy transfer

P. Biswas, L. N. Cella, S. H. Kang, A. Mulchandani, M. V. Yates and W. Chen, Chem. Commun., 2011, 47, 5259 DOI: 10.1039/C1CC10648A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements