Home

About

Advanced Search

Browse by Discipline

Scientific Societies

E-print Alerts

Add E-prints

E-print Network
FAQHELPSITE MAPCONTACT US


  Advanced Search  

 
1442 Biochemical Society Transactions (2008) Volume 36, part 6 iPEP: peptides designed and selected for
 

Summary: 1442 Biochemical Society Transactions (2008) Volume 36, part 6
iPEP: peptides designed and selected for
interfering with protein interaction and function
Jody M. Mason*1
, Kristian M. M šuller* and Katja M. Arndt*2
*Department of Biology, Albert-Ludwigs University of Freiburg, D79104 Freiburg, Germany, Center for Biological Signaling Studies (bioss), Albert-Ludwigs
University of Freiburg, D79104 Freiburg, Germany, and FRIAS, School of Life Sciences ­ LIFENET, Albert-Ludwigs University of Freiburg, Albertstrasse 19,
79104 Freiburg, Germany
Abstract
Semi-rational design is combined with PCAs (protein-fragment complementation assays) and phage-display
screening techniques to generate a range of iPEPs (interfering peptides) that target therapeutically relevant
proteins with much higher interaction stability than their native complexes. PCA selection has been improved
to impose a competitive and negative design initiative on the library screen, thus simultaneously improving
the specificity of assay `winners'. The folding pathways of designed pairs imply that early events are
dominated by hydrophobic collapse and helix formation, whereas later events account for the consolidation
of more intricate intermolecular electrostatic interactions.
Introduction
Is it possible to design proteins that can recognize and bind to
each other in both a stable and specific manner? Answering
this question is of importance not only in mapping of

  

Source: Arndt, Katja - Institut für Biologie III, Albert-Ludwigs-Universität Freiburg
Li, Haizhong - Department of Mathematical Sciences, Tsinghua University

 

Collections: Biology and Medicine; Biotechnology; Mathematics