An essential role of disulfide bonds for the hierarchical self-assembly and underwater affinity of CP20-derived peptides.

ABSTRACT: Barnacles are typical fouling organisms strongly adhere to immersed solid substrates by secreting proteinaceous adhesives called cement proteins (CPs). The self-assembly of the CPs forms a permanently bonded layer that binds barnacles to foreign surfaces. However, it is difficult to determine their natural structure and describe their self-assembly properties due to the abundance of cysteines in whole-length CP20. A putative functional motif of Balanus albicostatus CP20 (BalCP20) was identified to present distinctive self-assembly and wet-binding characteristics. Atomic-force microscopy (AFM) and transmission electron microscope (TEM) investigations showed that wildtype BalCP20-P3 formed grain-like spindles, which assembled into fractal-like structures like ears of wheat. SDS-PAGE,

SUBMITTER: Li B 

PROVIDER: S-EPMC9597634 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature