De Novo Design of Peptides that Co-assemble into β-sheet Based Nanofibrils Dataset

Author(s)
Xiao, Xingqing
Wang, Yiming
Seroski, Dillon T.
Wong, Kong M.
Liu, Renjie
Hudalla, Gregory A.
Hall, Carol K.
Advisor(s)
Editor(s)
Associated Organization(s)
Organizational Unit
School of Chemical and Biomolecular Engineering
School established in 1901 as the School of Chemical Engineering; in 2003, renamed School of Chemical and Biomolecular Engineering
Organizational Unit
Series
Supplementary to:
Abstract
Peptides’ hierarchical co-assembly into nanostructures enables controllable fabrication of multicomponent biomaterials. In this work, we describe a novel computational and experimental approach to design pairs of charge-complementary peptides that selectively co-assemble into β-sheet nanofibers when mixed together, but remain unassembled when isolated separately. The key advance is a pep_tide _c_o-_a_ssembly _d_esign (PepCAD) algorithm that searches for pairs of co-assembling peptides. Six peptide pairs are identified from a pool of ~106 candidates via the PepCAD algorithm and then subjected to DMD/PRIME20 simulations to examine their co-/self-association kinetics. The five pairs that spontaneously aggregate in kinetic simulations selectively co-assemble in biophysical experiments, with four forming β-sheet nanofibers, and one forming a stable non-fibrillar aggregate. Solid-state NMR, which is applied to characterize the co-assembling pairs, suggests that the _in-silico peptides exhibit a higher degree of structural order than the previously reported CATCH(+/-) peptides.
Sponsor
National Science Foundation Division of Chemical, Bioengineering, Environmental and Transport Systems Grant 1743432; National Science Foundation Division of Advanced Cyberinfrastructure Grant 1548562
Date
2021
Extent
Resource Type
Dataset
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Rights Statement
Creative Commons Attribution 4.0 International