Correlating topography and elastic properties of Elastin-Like Polypeptide scaffolds probed at the nanoscale: Intermodulation Atomic Force Microscopy experiments and Molecular Dynamic simulations

The synthesis and property characterization of soft biomaterials has taken precedence in recent years. Although bulk physical-chemical properties are well known for these bio-materials, nanoscale properties still need to be probed and evaluated to fine tune the bio-compatibility (structural as well as functional) with natural tissues for regenerative medicine, prosthetics and other biological applications. In this study, we focus on a popular soft biomaterial, ELastin-like polypeptide (ELP) which has been prepared under different pH conditions. We explore the topographical features of the ELP at the nanoscale using Atomic Force Microscopy (AFM). Additionally, we employ a non linear mode of AFM called Intermodulation-AFM (ImAFM) to correlate the elastic properties (Young's modulus) of ELP probed at the nanoscale with the topographical features which gives us a deep insight into the mechanical properties offered by ELP when the structural features are altered by change in the ELP synthesis conditions. The noteworthy point is that we measure theses properties at a spatial resolution of 0.9 nm. Finally, we explain the change in the structural features of ELP with varying pH through atomistic Molecular Dynamics Simulations. We follow the interaction mechanisms of the amino acid sequences and crosslinkers with proteins as they form the backbone and sidechain of the ELP at different pH.