Ca2+-induced self-assembly of Bombyx mori silk sericin into a nanofibrous network-like protein matrix for directing controlled nucleation of hydroxylapatite nano-needles. Issue 12 (17th February 2015)
- Record Type:
- Journal Article
- Title:
- Ca2+-induced self-assembly of Bombyx mori silk sericin into a nanofibrous network-like protein matrix for directing controlled nucleation of hydroxylapatite nano-needles. Issue 12 (17th February 2015)
- Main Title:
- Ca2+-induced self-assembly of Bombyx mori silk sericin into a nanofibrous network-like protein matrix for directing controlled nucleation of hydroxylapatite nano-needles
- Authors:
- Yang, Mingying
Zhou, Guanshan
Shuai, Yajun
Wang, Jie
Zhu, Liangjun
Mao, Chuanbin - Abstract:
- Abstract : Ca 2+ binding induces self-assembly of sericin into a nanofibrous network and the subsequent mineralization for promoting osteogenic differentiation of BMSCs. Abstract : Bone biomineralization is a well-regulated protein-mediated process where hydroxylapatite (HAP) crystals are nucleated with preferred orientation within the 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-assembledBS matrix. We found thatBS, rich in anionic amino acid residues, could bind Ca 2+ ions from the HAP precursor solution through electrostatic attraction. The Ca 2+ binding drove the conformational change ofBS from random coils into β-sheets and its concomitant self-assembly into the interconnected nanofibrous network-like protein matrix, which initiated the nucleation and growth of HAP crystals. HAP crystals directed by the resultant self-assembledBS matrix grew preferentially along their crystallographic c -axis, leading to the formation of HAP nano-needles. The HAP nano-needles in the self-assembledBS matrixAbstract : Ca 2+ binding induces self-assembly of sericin into a nanofibrous network and the subsequent mineralization for promoting osteogenic differentiation of BMSCs. Abstract : Bone biomineralization is a well-regulated protein-mediated process where hydroxylapatite (HAP) crystals are nucleated with preferred orientation within the 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-assembledBS matrix. We found thatBS, rich in anionic amino acid residues, could bind Ca 2+ ions from the HAP precursor solution through electrostatic attraction. The Ca 2+ binding drove the conformational change ofBS from random coils into β-sheets and its concomitant self-assembly into the interconnected nanofibrous network-like protein matrix, which initiated the nucleation and growth of HAP crystals. HAP crystals directed by the resultant self-assembledBS matrix grew preferentially along their crystallographic c -axis, leading to the formation of HAP nano-needles. The HAP nano-needles in the self-assembledBS matrix were subsequently aggregated into globules, probably driven by the hydrogen bonding between CO groups ofBS and O–H groups of HAP nano-needles. The present work sheds light on the chemical mechanisms ofBS self-assembly and the controlled mineralization directed by the self-assembled matrix. We also found that the resultant nanocomposites could promote the osteogenic differentiation of human bone marrow-derived mesenchymal stem cells. Thus our work also generates a biomimetic approach to bone-like silk protein/mineral nanocomposite scaffolds that can find potential applications in bone repair and regeneration. … (more)
- Is Part Of:
- Journal of materials chemistry. Volume 3:Issue 12(2015)
- Journal:
- Journal of materials chemistry
- Issue:
- Volume 3:Issue 12(2015)
- Issue Display:
- Volume 3, Issue 12 (2015)
- Year:
- 2015
- Volume:
- 3
- Issue:
- 12
- Issue Sort Value:
- 2015-0003-0012-0000
- Page Start:
- 2455
- Page End:
- 2462
- Publication Date:
- 2015-02-17
- Subjects:
- Materials -- Periodicals
Chemistry, Analytic -- Periodicals
Biomedical materials -- Research -- Periodicals
543.0284 - Journal URLs:
- http://pubs.rsc.org/en/journals/journalissues/tb# ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c4tb01944j ↗
- Languages:
- English
- ISSNs:
- 2050-750X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5012.205200
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 4926.xml