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Abstract The conformation of macromolecules attached to a surface is influenced by both their excluded volume and steric forces. Here, self‐avoiding random walk simulations are used to evaluate the occurrence of various conformations as a function of the number of monomeric units to estimate the effect of conformational entropy of a tethered chain. Then, a more realistic scenario is assessed, which can more accurately reproduce the shape of a tethered macromolecule. The simulations presented here confirm that it is more likely for a polymer to undergo a collapse conformation rather than a stretched one, as a collapse conformation can be realized in more different ways. Also, they confirm the “mushroom” shape of polymers close to a surface. From this simple approach, the conformation entropy of a model 100‐unit polymer close to a surface is estimated to contribute with over 129 toward its collapse. This conformation entropy is higher than that of typical hydrogen bonds and even barriers that keep proteins folded. As such, entropic collapse of macromolecules plays an important role in realizing the mushroom shape of attached polymers and can be the driving force in protein folding, while the polypeptide chain emerges from the ribosome. 

Abstract Programmable behavior combined with tailored stiffness and tunable biomechanical response are key requirements for developing successful materials. However, these properties are still an elusive goal for protein-based biomaterials. Here, we use protein-polymer interactions to manipulate the stiffness of protein-based hydrogels made from bovine serum albumin (BSA) by using polyelectrolytes such as polyethyleneimine (PEI) and poly-L-lysine (PLL) at various concentrations. This approach confers protein-hydrogels with tunable wide-range stiffness, from ~10–64 kPa, without affecting the protein mechanics and nanostructure. We use the 6-fold increase in stiffness induced by PEI to program BSA hydrogels in various shapes. By utilizing the characteristic protein unfolding we can induce reversible shape-memory behavior of these composite materials using chemical denaturing solutions. The approach demonstrated here, based on protein engineering and polymer reinforcing, may enable the development and investigation of smart biomaterials and extend protein hydrogel capabilities beyond their conventional applications. 

DLC1 locks talin R8 in a mechanically stable state, potentially preventing the inside-out activation of integrins.