@article{dong_liu_seroski_hudalla_hall_2023, title={Programming co-assembled peptide nanofiber morphology via anionic amino acid type: Insights from molecular dynamics simulations}, volume={19}, ISSN={["1553-7358"]}, DOI={10.1371/journal.pcbi.1011685}, abstractNote={Co-assembling peptides can be crafted into supramolecular biomaterials for use in biotechnological applications, such as cell culture scaffolds, drug delivery, biosensors, and tissue engineering. Peptide co-assembly refers to the spontaneous organization of two different peptides into a supramolecular architecture. Here we use molecular dynamics simulations to quantify the effect of anionic amino acid type on co-assembly dynamics and nanofiber structure in binary CATCH(+/-) peptide systems. CATCH peptide sequences follow a general pattern: CQCFCFCFCQC, where all C’s are either a positively charged or a negatively charged amino acid. Specifically, we investigate the effect of substituting aspartic acid residues for the glutamic acid residues in the established CATCH(6E-) molecule, while keeping CATCH(6K+) unchanged. Our results show that structures consisting of CATCH(6K+) and CATCH(6D-) form flatter β-sheets, have stronger interactions between charged residues on opposing β-sheet faces, and have slower co-assembly kinetics than structures consisting of CATCH(6K+) and CATCH(6E-). Knowledge of the effect of sidechain type on assembly dynamics and fibrillar structure can help guide the development of advanced biomaterials and grant insight into sequence-to-structure relationships.}, number={12}, journal={PLOS COMPUTATIONAL BIOLOGY}, author={Dong, Xin and Liu, Renjie and Seroski, Dillon T. and Hudalla, Gregory A. and Hall, Carol K.}, year={2023}, month={Dec} }
 @article{wong_robang_lint_wang_dong_xiao_seroski_liu_shao_hudalla_et al._2021, title={Engineering beta-Sheet Peptide Coassemblies for Biomaterial Applications}, volume={12}, ISSN={["1520-5207"]}, DOI={10.1021/acs.jpcb.1c04873}, abstractNote={Peptide coassembly, wherein at least two different peptides interact to form multicomponent nanostructures, is an attractive approach for generating functional biomaterials. Current efforts seek to design pairs of peptides, A and B, that form nanostructures (e.g., β-sheets with ABABA-type β-strand patterning) while resisting self-assembly (e.g., AAAAA-type or BBBBB-type β-sheets). To confer coassembly behavior, most existing designs have been based on highly charged variants of known self-assembling peptides; like-charge repulsion limits self-assembly while opposite-charge attraction promotes coassembly. Recent analyses using solid-state NMR and coarse-grained simulations reveal that preconceived notions of structure and molecular organization are not always correct. This perspective highlights recent advances and key challenges to understanding and controlling peptide coassembly.}, journal={JOURNAL OF PHYSICAL CHEMISTRY B}, author={Wong, Kong M. and Robang, Alicia S. and Lint, Annabelle H. and Wang, Yiming and Dong, Xin and Xiao, Xingqing and Seroski, Dillon T. and Liu, Renjie and Shao, Qing and Hudalla, Gregory A. and et al.}, year={2021}, month={Dec} }
 @article{seroski_dong_wong_liu_shao_paravastu_hall_hudalla_2020, title={Charge guides pathway selection in beta-sheet fibrillizing peptide co-assembly}, volume={3}, ISSN={["2399-3669"]}, DOI={10.1038/s42004-020-00414-w}, abstractNote={Abstract}, number={1}, journal={COMMUNICATIONS CHEMISTRY}, author={Seroski, Dillon T. and Dong, Xin and Wong, Kong M. and Liu, Renjie and Shao, Qing and Paravastu, Anant K. and Hall, Carol K. and Hudalla, Gregory A.}, year={2020}, month={Nov} }