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In biology, there are several processes in which unfolded protein chains aretransported along narrow-tube channels. Normally, without such a severeconfigurational constraint, unfolded polypeptides would not bind to each other.However, when chain entropy is much reduced in the narrow channel, we find thatpolypeptide chains have a propensity to bind, even if there is no greatpotential energy gain in doing so. We find the average length of binding m*(the number of monomers at the chain ends that form bonds) and the criticaltube diameter at which such constrained binding occurs. We carry out Browniandynamics simulations of tightly confined chains, demonstrating their bindingover the characteristic length m*, changing in tubes of different diameter.

Stimulated binding of polymer chains by narrow tube confinement