Protein–protein interactions (PPIs) are involved in many cellular processes; consequently, the discovery of small molecules as modulators of PPIs has become an important challenge in medicinal chemistry. Structural mimetics of α‐helices, β‐turns or β‐strands could maintain or restore biological functions and should possess biological activity. At this time, the most challenging classes of PPIs are those mediated by β‐sheet interactions, which are implicated in a number of diseases. Only a few β‐strand mimics have been published to date. This study presents an evaluation of oligothienylpyridyl scaffolds in view of their ability for β‐strand mimicry. In this study, theoretical ring twist angle predictions for these scaffolds have been validated by X‐ray diffraction and molecular dynamics simulations with NMR constraints. Careful choice of substituent and heavy‐atom positions in the foldamer units opens the way to produce reasonably coplanar compounds mimicking β‐strand side‐chain distribution