ArticleIranian journal of biotechnology2019
Straightforward and Cost-Effective Production of RADA-16I Peptide in
Article in Iranian journal of biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- Advances in the development and optimization strategies of the hemostatic biomaterials.Frontiers in bioengineering and biotechnology · 2022Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundRADA16I represents one of promising hydrogel forming peptides. Several implementations of RADA16I hydrogels have proven successful in the field of regenerative medicine and tissue engineering. However, RADA16I peptides used in various studies utilize synthetic peptides and so far, only two research articles have been published on RADA16I peptide recombinant production. Moreover, previous studies utilized non- or less routine expression and purification methods to produce RADA16I peptide recombinantly.
objectivesThe main goal was to produce the self-assembling peptide, RADA16I, in MATERIAL AND
methodsRADA16I coding sequence was inserted in pET31b+, and the construct was transformed into E. coli. Purified fusion constructs were purified using Nickel Sepharose. RADA16I unimers were released using CNBr cleavage. CD and FTIR spectroscopy were used to study recombinant RADA16I's confirmation. TEM was used to confirm fibril formation of recombinant RADA16I. Furthermore, MTT assay was implemented to assess cytocompatibility of recombinant RADA16I.
resultsThe biochemical, biophysical and structural analysis proved the ability of the recombinant RADA16I to form self-assembling peptide nanofibers. Furthermore, the nanofibers exhibited no cytotoxicity and retained their cell adhesive activity.
conclusionsWe successfully produced RADA16I in acceptable levels and established a basis for future investigation for the production of RADA16I under fermentation conditions.
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Registered trials
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