Molecular design and modeling of protein heparin interactions

Abstract The methods and approaches taken to investigate heparin-apoE peptide interactions have involved a series of steps, including (1) identification of the heparin-binding domains of apoE, (2) determination of the minimal amino acid sequence regions involved in heparin binding, heparin-induced conformational changes, and stability of apoE peptide structures in solution, (3) modeling of these peptide and oligosaccharide structures, and (4) examination of their behavior during molecular dynamics calculations to determine if the modeled complexes simulate the results of the solution study.