To expand the scope of potential applications of EAK16-II (EAK) fibrils in physiological locales with limited fluids, we have generated a method by which EAK fibrils are pre-assembled yet remain injectable. EAK is a self-assembling peptide (SAP) that forms β-sheets and β-fibrils through ionic-complementary interactions at physiological ionic strengths. In order to pre-assemble the fibrils outside of the aforementioned conditions, we used the carbodiimide cross-linker, N-ethyl-N’-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) to induce the formation of amide bonds between glutamate and lysine residues in the EAK peptides and β-sheets. Using Diffuse Reflectance Infrared Fourier Transform (DRIFT) spectroscopy, Scanning Electron Microscopy (SEM), and Atomic Force Microscopy (AFM) we were able to determine that the addition of EDC to EAK causes a 3-dimensional (3D) matrix to form, facilitated by the additional amide cross-links, enhancing the stacking of b-sheet bilayers. The cross-linked EAK (clEAK) was shown to trap polymeric microspheres with an average diameter of 1 µm. Macrophages admixed with clEAK were found to be viable and did not produce IL-1β, demonstrating that the matrix has low inflammatory potential. These results indicate that clEAK should be explored as a platform for delivering drugs and cells <i>in vivo</i>.

Chemically-induced cross-linking of peptidic fibrils for scaffolding polymeric particles and macrophages

ACS Spring Meeting 2021

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.