title: Aromatic-Aromatic Interactions Enable α-Helix to β-Sheet Transition of Peptides to Form Supramolecular Hydrogels.
abstract: Isolated short peptides usually are unable to maintain their original secondary structures due to the lack of the restriction from proteins. Here we show that two complementary pentapeptides from a β-sheet motif of a protein, being connected to an aromatic motif (i.e., pyrene) at their C-terminal, self-assemble to form β-sheet like structures upon mixing. Besides enabling the self-assembly to result in supramolecular hydrogels upon mixing, aromatic-aromatic interactions promote the pentapeptides transform from α-helix to β-sheet conformation. As the first example of using aromatic-aromatic interactions to mimic the conformational restriction in a protein, this work illustrates a bioinspired way to generate peptide nanofibers with predefined secondary structures of the peptides by a rational design using protein structures as the blueprint.
authors.affiliation: Department of Chemistry, Brandeis University , 415 South Street, Waltham, Massachusetts 02454, United States.
authors.forename: Jie
authors.initials: J
authors.lastname: Li
authors.affiliation: Department of Chemistry, Brandeis University , 415 South Street, Waltham, Massachusetts 02454, United States.
authors.forename: Xuewen
authors.initials: X
authors.lastname: Du
authors.affiliation: Department of Chemistry, Brandeis University , 415 South Street, Waltham, Massachusetts 02454, United States.
authors.forename: Saqib
authors.initials: S
authors.lastname: Hashim
authors.affiliation: Department of Chemistry, Brandeis University , 415 South Street, Waltham, Massachusetts 02454, United States.
authors.forename: Adrianna
authors.initials: A
authors.lastname: Shy
authors.affiliation: Department of Chemistry, Brandeis University , 415 South Street, Waltham, Massachusetts 02454, United States.
authors.forename: Bing
authors.identifier: 0000-0002-4639-387X
authors.initials: B
authors.lastname: Xu
mesh_terms: D020100:Hydrogels / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand
chemical_list: D020100:Hydrogels; D010455:Peptides