Recombinant DNA technology and click chemistry: a powerful combination for generating a hybrid elastin-like-statherin hydrogel to control calcium phosphate mineralization
- Understanding the mechanisms responsible for generating different phases and morphologies of calcium phosphate by elastin-like recombinamers is supreme for bioengineering of advanced multifunctional materials. The generation of such multifunctional hybrid materials depends on the properties of their counterparts and the way in which they are assembled. The success of this assembly depends on the different approaches used, such as recombinant DNA technology and click chemistry. In the present work, an elastin-like recombinamer bearing lysine amino acids distributed along the recombinamer chain has been cross-linked via Huisgen [2 + 3] cycloaddition. The recombinamer contains the SN(A)15 peptide domains inspired by salivary statherin, a peptide epitope known to specifically bind to and nucleate calcium phosphate. The benefit of using click chemistry is that the hybrid elastin-like-statherin recombinamers cross-link without losing their fibrillar structure. Mineralization of the resulting hybrid elastin-like-statherin recombinamerUnderstanding the mechanisms responsible for generating different phases and morphologies of calcium phosphate by elastin-like recombinamers is supreme for bioengineering of advanced multifunctional materials. The generation of such multifunctional hybrid materials depends on the properties of their counterparts and the way in which they are assembled. The success of this assembly depends on the different approaches used, such as recombinant DNA technology and click chemistry. In the present work, an elastin-like recombinamer bearing lysine amino acids distributed along the recombinamer chain has been cross-linked via Huisgen [2 + 3] cycloaddition. The recombinamer contains the SN(A)15 peptide domains inspired by salivary statherin, a peptide epitope known to specifically bind to and nucleate calcium phosphate. The benefit of using click chemistry is that the hybrid elastin-like-statherin recombinamers cross-link without losing their fibrillar structure. Mineralization of the resulting hybrid elastin-like-statherin recombinamer hydrogels with calcium phosphate is described. Thus, two different hydroxyapatite morphologies (cauliflower- and plate-like) have been formed. Overall, this study shows that crosslinking elastin-like recombinamers leads to interesting matrix materials for the generation of calcium phosphate composites with potential applications as biomaterials.…
Author details: | Mohamed Hamed Misbah, Mercedes SantosORCiD, Luis Quintanilla, Christina GünterGND, Matilde Alonso, Andreas TaubertORCiDGND, Jose Carlos Rodriguez-Cabello |
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DOI: | https://doi.org/10.3762/bjnano.8.80 |
ISSN: | 2190-4286 |
Pubmed ID: | https://pubmed.ncbi.nlm.nih.gov/28487820 |
Title of parent work (English): | Beilstein journal of nanotechnology |
Publisher: | Beilstein-Institut zur Förderung der Chemischen Wissenschaften |
Place of publishing: | Frankfurt, Main |
Publication type: | Article |
Language: | English |
Year of first publication: | 2017 |
Publication year: | 2017 |
Release date: | 2020/04/20 |
Tag: | SN(A)15; calcium phosphate; elastin-like recombinamers; hydroxyapatite; mineralization |
Volume: | 8 |
Number of pages: | 12 |
First page: | 772 |
Last Page: | 783 |
Funding institution: | European Commission [NMP-2014-646075, HEALTH-F4-2011-278557, PITN-GA-2012-317306, MSCA-ITN-2014642687]; MINECO of the Spanish Government [MAT2013-42473-R, MAT2013-41723-R]; Junta de Castilla y Leon, Spain [VA244U13, VA313U14, GRS/516/A/10]; Deutsche Forschungsgemeinschaft (DFG) [TA571/11-1]; University of Potsdam |
Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Geowissenschaften |
Peer review: | Referiert |