More unique and efficient biomaterials are being discovered that allow tissue engineering to be successful and progress onward as well. A research team part of the Indian Institute of Technology (IIT) recently found that silk protein fibroin works well with tissue engineering and drug delivery.
The chemical structure of silk protein fibroin is what contributes to its great value in these bioengineering applications. We wrote about silk from spiders and its use to create artificial hearts in a previous blog post. Similarly, silk fibroin is a protein that comes from moth genera, such as spiders. Proteins consist of amino acids (as we learned in biology last year!). Silk consists of, specifically, 60% Glycine, 20% Alanine, and 20% Serine.
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| Silk Fibroin structure |
These IIT researchers utilized a combination of silk fibroin and the protein albumin in order to provide an overall stronger material.
Electrostatic interactions exist among the silk fibroin's carboxyl groups and the amino groups of albumin.
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| Albumin structure |
Amino groups, being positively charged, attracts to the negatively charged carboxyl groups, creating a strong combination of electrostatic interactions because opposite charges attract. This strength contributes to the "encapsulation" and "drug retention" of the drug.
These researchers then created fibroin-blended nanoparticles. FITC (Fluoresceine-isothiocyante) nanparticles are not toxic to body cells, which they can reach. When
methotrexate, another drug, is added to the fibroin-blended nanoparticles, delayed drug release increases.
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| Methotrexate structure |
Additionally, the nanoparticles are able to remain at a site longer, which may allow them to be used with methotrexate as nanocarriers or hydrophobic therapeutic agents.
http://nanotechweb.org/cws/article/lab/52196
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