A novel peptide isolated from Catla skin collagen acts as a self-assembling scaffold promoting nucleation of calcium-deficient hydroxyapatite nanocrystals. (9th December 2022)
- Record Type:
- Journal Article
- Title:
- A novel peptide isolated from Catla skin collagen acts as a self-assembling scaffold promoting nucleation of calcium-deficient hydroxyapatite nanocrystals. (9th December 2022)
- Main Title:
- A novel peptide isolated from Catla skin collagen acts as a self-assembling scaffold promoting nucleation of calcium-deficient hydroxyapatite nanocrystals
- Authors:
- Asokan, Vishwadeep
Yelleti, Geethika
Bhat, Chetna
Bajaj, Mayur
Banerjee, Pradipta - Abstract:
- Abstract: Catla collagen hydrolysate (CH) was fractionated by chromatography and each fraction was subjected to HA nucleation, with the resultant HA-fraction composites being scored based on the structural and functional group of the HA formed. The process was repeated till a single peptide with augmented HA nucleation capacity was obtained. The peptide (4.6 kDa), exhibited high solubility, existed in polyproline-II conformation and displayed a dynamic yet stable hierarchical self-assembling property. The 3D modelling of the peptide revealed multiple calcium and phosphate binding sites and a high propensity to self-assemble. Structural analysis of the peptide-HA crystals revealed characteristic diffraction planes of HA with mineralization following the (002) plane, retention of the self-assembled hierarchy of the peptide and intense ionic interactions between carboxyl groups and calcium. The peptide-HA composite crystals were mostly of 25–40 nm dimensions and displayed 79% mineralization, 92% crystallinity, 39.25% porosity, 12GPa Young's modulus and enhanced stability in physiological pH. Cells grown on peptide-HA depicted faster proliferation rates and higher levels of osteogenic markers. It was concluded that the prerequisite for HA nucleation by a peptide included: a conserved sequence with a unique charge topology allowing calcium chelation and its ability to form a dynamic self-assembled hierarchy for crystal propagation. Graphical Abstract:
- Is Part Of:
- Journal of biochemistry. Volume 173:Number 3(2023)
- Journal:
- Journal of biochemistry
- Issue:
- Volume 173:Number 3(2023)
- Issue Display:
- Volume 173, Issue 3 (2023)
- Year:
- 2023
- Volume:
- 173
- Issue:
- 3
- Issue Sort Value:
- 2023-0173-0003-0000
- Page Start:
- 197
- Page End:
- 224
- Publication Date:
- 2022-12-09
- Subjects:
- structure -- self-assembly -- nano-hydroxyapatite -- collagen peptide -- biomimetic synthesis
Biochemistry -- Periodicals
Biochemistry -- Periodicals
Electronic journals
572.05 - Journal URLs:
- http://wwwsoc.nii.ac.jp/jbiochem/jb/index.htm ↗
http://jb.oupjournals.org/ ↗
http://jb.oxfordjournals.org/ ↗
http://www.bcasj.or.jp/jbindex.html ↗
http://ukcatalogue.oup.com/ ↗ - DOI:
- 10.1093/jb/mvac103 ↗
- Languages:
- English
- ISSNs:
- 0021-924X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4952.000000
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British Library HMNTS - ELD Digital store - Ingest File:
- 26172.xml