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Published online on February 6, 2007, 10.1073/pnas.0611610104
PNAS | February 13, 2007 | vol. 104 | no. 7 | 2029-2030


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COMMENTARY
Probing the interactions of proteins and nanoparticles

Jacob Klein*

Department of Physical and Theoretical Chemistry, Oxford University, Oxford OX1 3QZ, United Kingdom; and Materials and Interfaces Department, Weizmann Institute of Science, Rehovot 76100, Israel

Despite the hype concerning the vast and imminent commercial potential of nanotechnology, there is little doubt that nanoparticles offer real and radically new opportunities in fields such as biomedicine and materials science (1, 2), among others. Such particles are small enough to enter almost all areas of the body, including cells and organelles, potentially leading to a new approach to medicine (nanomedicine), including rational approaches to targeted intracellular delivery of genes and other therapies (see, e.g., ref. 3). However, there have been widespread concerns that their use could involve some biological hazard (4–8) and a growing consensus that our understanding of the interaction of nanoscale objects with living matter, even at the level of single cells, has not kept pace with the explosive development of nanoscience in the past decades. A significant step in this area has been taken by Cedervall et al. (9) in this issue of PNAS on development of methods for probing the association of proteins to nanoparticles: Such association is almost always a first step when nanoparticles enter a biological fluid, so that when we think of the interactions of nanoparticles with a living system, we are really speaking of protein-coated particles. Adsorption of the proteins onto the particle surface can lead to altered conformation, exposure of novel "cryptic" peptide epitopes, perturbed function (caused by structural effects or local high concentration), or avidity effects arising from the close spatial repetition of the same protein (10). Thus, although protein adsorption has been studied classically both on planar surfaces and in colloidal dispersions (11–13), the focus by Cedervall et al. on the specific binding rates and affinities of different plasma-related proteins to nanoparticles is a welcome development in this field. . . . [Full Text of this Article]

*E-mail: jacob.klein@chem.ox.ac.uk or jacob.klein@weizmann.ac.il


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Companion article to this Commentary:

From the Cover: Understanding the nanoparticle–protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles
Tommy Cedervall, Iseult Lynch, Stina Lindman, Tord Berggård, Eva Thulin, Hanna Nilsson, Kenneth A. Dawson, and Sara Linse
PNAS 2007 104: 2050-2055. [Abstract] [Full Text]  





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