Unknown

Dataset Information

0

Amphiphilic Histidine-Based Oligopeptides Exhibit pH-Reversible Fibril Formation.


ABSTRACT: We report the design, simulation, synthesis, and reversible self-assembly of nanofibrils using polyhistidine-based oligopeptides. The inclusion of aromatic amino acids in the histidine block produces distinct antiparallel β-strands that lead to the formation of amyloid-like fibrils. The structures undergo self-assembly in response to a change in pH. This creates the potential to produce well-defined fibrils for biotechnological and biomedical applications that are pH-responsive in a physiologically relevant range.

SUBMITTER: Noble Jesus C 

PROVIDER: S-EPMC8375021 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC5456802 | biostudies-other
| S-EPMC5625065 | biostudies-literature
| S-EPMC4142984 | biostudies-literature
| S-EPMC6643022 | biostudies-literature
| S-EPMC4426459 | biostudies-literature
| S-EPMC3568905 | biostudies-literature
| S-EPMC7187140 | biostudies-literature
| S-EPMC3458612 | biostudies-literature
| S-EPMC8254510 | biostudies-literature
| S-EPMC8512540 | biostudies-literature