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Selection of Peptides Interfering with ProteinProtein Interaction
 

Summary: Chapter 16
Selection of Peptides Interfering with Protein­Protein
Interaction
Annette Gaida, Urs B. Hagemann, Dinah Mattay, Christina Ra¨uber,
Kristian M. Mu¨ller, and Katja M. Arndt
Abstract
Cell physiology depends on a fine-tuned network of protein­protein interactions, and misguided interac-
tions are often associated with various diseases. Consequently, peptides, which are able to specifically
interfere with such adventitious interactions, are of high interest for analytical as well as medical purposes.
One of the most abundant protein interaction domains is the coiled-coil motif, and thus provides a premier
target. Coiled coils, which consist of two or more -helices wrapped around each other, have one of the
simplest interaction interfaces, yet they are able to confer highly specific homo- and heterotypic interactions
involved in virtually any cellular process. While there are several ways to generate interfering peptides, the
combination of library design with a powerful selection system seems to be one of the most effective and
promising approaches. This chapter guides through all steps of such a process, starting with library options
and cloning, detailing suitable selection techniques and ending with purification for further down-stream
characterization. Such generated peptides will function as versatile tools to interfere with the natural
function of their targets thereby illuminating their down-stream signaling and, in general, promoting
understanding of factors leading to specificity and stability in protein­protein interactions. Furthermore,
peptides interfering with medically relevant proteins might become important diagnostics and therapeutics.

  

Source: Arndt, Katja - Institut für Biologie III, Albert-Ludwigs-Universität Freiburg

 

Collections: Biotechnology; Biology and Medicine