Novel Bovine Serum Albumin Protein Backbone Reassembly Study: Strongly Twisted ß-Sheet Structure Promotion upon Interaction with GO-PAMAM.

This study investigates the formation of a graphene oxide-polyamidoamine dendrimer complex (GO-PAMAM) and its association and interaction with bovine serum albumin (BSA). Fourier-transform infrared spectrometry and X-ray photoelectron spectrometry indicated the formation of covalent linkage between the GO surface and PAMAM with 7.22% nitrogen content in the GO-PAMAM sample, and various interactions between BSA and GO-PAMAM, including π-π* interactions at 291.5 eV for the binding energy value. Thermogravimetric analysis highlighted the increasing thermal stability throughout the modification process, from 151 to 192 °C for the 10% weight loss temperature. Raman spectrometry and X-ray diffraction analysis were used in order to examine the complexes' assembly, showing a prominent (0 0 2) lattice in GO-PAMAM. Dynamic light scattering tests proved the formation of stable graphenic and graphenic-protein aggregates. The secondary structure rearrangement of BSA after interaction with GO-PAMAM was investigated using circular dichroism spectroscopy. We have observed a shift from 10.9% ß-sheet composition in native BSA to 64.9% ß-sheet composition after the interaction with GO-PAMAM. This interaction promoted the rearrangement of the protein backbone, leading to strongly twisted ß-sheet secondary structure architecture.