Abstract
The discovery of cell penetrating peptides (CPPs) opened new perspectives for the delivery of proteins into human cells. It is considered that in the future CPP-mediated transport of therapeutic proteins may find applications in the treatment of human diseases. Despite this fact a fast and simple method for the purification of CPP-tagged proteins, free of additional tags, was not available to date. To fill this gap we developed the Argi system for one-step purification of proteins tagged with arginine rich CPPs.
Highlights
Cell penetrating peptides (CPPs) are short peptides capable of traversing the plasma membrane
Particular attention has been given to studies of potential therapeutic application of cell penetrating peptides (CPPs)
To provide simple and fast purification of these proteins by affinity chromatography additional tags, e.g. His-tag can be fused with CPP-tagged proteins[8]
Summary
Cell penetrating peptides (CPPs) are short peptides capable of traversing the plasma membrane They can promote the transport of low and high molecular weight cargos, including peptides and proteins, into the cell[1]. Based on their biochemical properties CPPs are classified into three groups: (i) cationic, (ii) amphipathic and (iii) hydrophobic[2]. To overcome the current problems with the methodology of arginine-rich CPP-tagged protein purification, minimize the risk of a possible immune response against www.nature.com/scientificreports/. CPP-tagged therapeutics and to reduce the costs of CPP-tagged protein production in the future, we present here the development of the Argi system – a new affinity chromatography tool for one-step purification of arginine-rich CPP-tagged proteins. The presented system is based on the interaction between a DNA aptamer and arginine-rich CPPs
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
