Ca²⁺-induced self-assembly of Bombyx mori silk sericin into a nanofibrous network-like protein matrix for directing controlled nucleation of hydroxylapatite nano-needles.

ABSTRACT: Bone biomineralization is a well-regulated protein-mediated process where hydroxylapatite (HAP) crystals are nucleated with preferred orientation within self-assembled protein matrix. Mimicking this process is a promising approach to the production of bone-like protein/mineral nanocomposites for bone repair and regeneration. Towards the goal of fabricating such nanocomposites from sericin, a protein spun by Bombyx mori (B.mori) silkworm, and bone mineral HAP, for the first time we investigated the chemical mechanism underpinning the synergistic processes of the conformational change/self-assembly of B.mori sericin ( BS ) as well as the nucleation of HAP on the resultant self-assembled BS matrix. We found that BS , rich in anion

SUBMITTER: Yang M 

PROVIDER: S-EPMC4449145 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature