Skripsi
EKSPRESI PROTEIN REKOMBINAN CPP PADA ESCHERICHIA COLI
Background: Cell Penetrating Peptide (CPP) is a carrier system which usually consists of 5-30 amino acid residues and has been widely studied as a delivery vector for transporting RNA / DNA, plasmids, antibodies, and nanoparticles into cells. With the development of knowledge, analysis techniques in silico are very important to design, optimize recombinant protein expression in the host, and predict structure and even cellular activity of proteins. In this study, author conducted a literature study of CPP as a carrier medium and then by using in silico techniques construct and characterize the recombinant protein coding gene CPP (Penetratin) and predict the solubility of the resulting protein. This study aims to provide a bioinformatics analysis in order to predict the structure and relationship of CPP in Escherichia coli. Methods: This study is an experimental study with in silico approach. Data in the form of amino acid sequences were accessed from Pubmed and the iGEM registry. This study uses several website-based applications including OptimumGeneTM, Predict Protein, and Protein-SOL. Results: It was found that the secondary structure composition of CPP (Penetratin) was 24% beta-strand, 48% alpha-helix, and 28% loops predicted by using Predict Protein and the percentage of solvent accessibility was consists of 96% exposed proteins, 4% buried proteins. From Protein-SOL, it was found that the solubility of Penetratin protein was 0.751. Conclusion: From in silico analysis, it was concluded that recombinant protein penetratin has a dominant alpha-helix structure, has hydrophilic-dominant properties and also has a high protein solubility. Keywords: CPP, recombinant protein, in silico analysis
Inventory Code | Barcode | Call Number | Location | Status |
---|---|---|---|---|
2007000130 | T40495 | T404952020 | Central Library (REFERENCES) | Available but not for loan - Not for Loan |
No other version available