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Determining Binding Affinity KD of Radiolabeled Antibodies to Immobilized Antigens

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Affinity versus specificity in coupled binding and folding reactions.

Stefano Gianni¹, Per Jemth²

¹Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Istituto Pasteur-Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR, Sapienza Università di Roma, Rome 00185, Italy.

Protein Engineering, Design & Selection : PEDS

|August 10, 2019

Summary

This summary is machine-generated.

Intrinsically disordered protein regions (IDPRs) may not follow the typical stability-affinity trade-off. Instead of weakening binding, folding upon interaction can increase affinity and expand protein interaction networks.

Keywords:

protein binding protein disorder

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Area of Science:

Biochemistry
Structural Biology
Molecular Biology

Background:

Intrinsically disordered protein regions (IDPRs) are known to interact with binding partners.
A common hypothesis suggests coupled folding and binding in IDPRs leads to high specificity and low affinity.
This concept implies an unfavorable folding equilibrium weakens the overall binding interaction.

Purpose of the Study:

To re-evaluate the prevailing hypothesis regarding the role of folding in the affinity and specificity of intrinsically disordered protein regions.
To investigate the conformational dynamics of IDPRs during protein-protein interactions.
To explore the evolutionary advantages of IDPRs in protein interaction networks.

Main Methods:

Analysis of existing experimental evidence on IDPR interactions.
Conformational analysis of disordered regions in both free and bound states.
Evaluation of factors influencing affinity and specificity in IDPRs.

Main Results:

Experimental data indicate IDPRs often interact in extended conformations, not pre-folded states.
Folding upon binding can potentially increase the affinity of IDPRs, rather than decrease it.
Affinity and specificity are modulated by sequence-specific factors (side chains, length) and not solely by disorder.

Conclusions:

The concept of a stability-affinity trade-off for IDPRs may be misleading.
IDPRs likely increase the repertoire of binding partners, facilitating interaction evolution.
Disordered regions offer an accessible evolutionary route for new protein-protein interactions.