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Selection and characterisation of affibody molecules inhibiting the interaction between Ras and Raf in vitro

Paper ID Volume ID Publish Year Pages File Format Full-Text
33553 44984 2010 8 PDF Available
Title
Selection and characterisation of affibody molecules inhibiting the interaction between Ras and Raf in vitro
Abstract

Development of molecules with the ability to selectively inhibit particular protein–protein interactions is important in providing tools for understanding cell biology. In this work, we describe efforts to select small Ras- and Raf-specific three-helix bundle affibody binding proteins capable of inhibiting the interaction between H-Ras and Raf-1, from a combinatorial library displayed on bacteriophage. Target-specific variants with typically high nanomolar or low micromolar affinities (KD) could be selected successfully against both proteins, as shown by dot blot, ELISA and real-time biospecific interaction analyses. Affibody molecule variants selected against H-Ras were shown to bind epitopes overlapping each other at a site that differed from that at which H-Ras interacts with Raf-1. In contrast, an affibody molecule isolated during selection against Raf-1 was shown to effectively inhibit the interaction between H-Ras and Raf-1 in a dose-dependent manner. Possible intracellular applications of the selected affibody molecules are discussed.

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Selection and characterisation of affibody molecules inhibiting the interaction between Ras and Raf in vitro
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Publisher
Database: Elsevier - ScienceDirect
Journal: New Biotechnology - Volume 27, Issue 6, 31 December 2010, Pages 766–773
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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