Free energy perturbation simulations measure the change in binding affinity of the Aβ25–35 peptide to the zwitterionic bilayer caused by oxidation. Luo, X., Khayat, E., Bowers, S. R., Delfing, B. M., Lockhart, C., & Klimov, D. K. (2025) Free energy perturbation simulations measure the change in binding affinity of the Aβ25–35 peptide to the zwitterionic bilayer caused by oxidation. J. Chem. Inf. Model. (accepted) >
De novo transmembrane aggregation of Aβ10-40 peptides in anionic lipid bilayer. Vergilio, J., Lockhart, C., & Klimov, D. K. (2022) De novo transmembrane aggregation of Aβ10-40 peptides in anionic lipid bilayer. J. Chem. Inf. Model. 62(23): 6228-6241, doi: 10.1021/acs.jcim.2c01192
Mechanisms of binding of antimicrobial peptide PGLa to DMPC/DMPG membrane. Bowers, S. R., Klimov, D. K., & Lockhart, C. (2022) Mechanisms of binding of antimicrobial peptide PGLa to DMPC/DMPG membrane. J. Chem. Inf. Model. 62(6): 1525-1537, doi: 10.1021/acs.jcim.1c01518