Total synthesis of horse heart cytochrome C.
Abstract: A strategy based on complexation-assisted condensation of large synthetic protein fragments and mitochondria-mediated stereospecific heme insertion has been utilized to assemble a functional molecule corresponding to native horse heart holocytochrome c. This original approach offers the unique opportunity of selective modifications both in the C-terminal and in the N-terminal regions of the apoprotein and may represent an useful alternative to site-directed mutagenesis, particularly when D-amino acids, chemically and/or isotopically modified or other unnatural amino acids have to be introduced in this important molecule. The present result is an example of how solid phase peptide synthesis of large protein fragments in conjunction with the availability of a specific recognition process may extend the potentiality of the chemical approach to the synthesis of an entire protein.
Publication Date: 1992-02-28 PubMed ID: 1311923DOI: 10.1016/0006-291x(92)91637-6Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research paper outlines a novel strategy for the total synthesis of the protein, horse heart cytochrome c, using a combination of complexation-assisted condensation of large synthetic protein fragments and mitochondria-mediated heme insertion.
Research Methodology
- The study employed a strategy known as complexation-assisted condensation, a method that brings together large synthetic protein fragments. This method is often used in protein synthesis as it enables the creation of large molecules from smaller fragments.
- The researchers also used mitochondria-mediated heme insertion. This method is typically employed in the synthesis of proteins that require the insertion of heme groups. Heme groups are a type of iron-containing molecule that are key to certain biological functions.
Novel Strategy for Protein Synthesis
- The researchers have innovated a new approach that could help modify specific sections – both the C-terminal and N-terminal regions – of the apoprotein.
- This approach may serve as a viable alternative to site-directed mutagenesis, a common method of genetically modifying an organism’s DNA. This is particularly significant when D-amino acids or other unnatural amino acids need to be introduced in the molecule which are chemically and/or isotopically modified.
Implications of the Study
- The findings demonstrate that solid-phase peptide synthesis of these large protein fragments, coupled with the availability of a specific recognition process, may increase the reach of the chemical approach to synthesize an entire protein.
- Given the importance of such proteins in various biochemical reactions and pathways, this research could have significant implications for the study of biochemical processes and for the development of related technologies and medical treatments.
Cite This Article
APA
Di Bello C, Vita C, Gozzini L.
(1992).
Total synthesis of horse heart cytochrome C.
Biochem Biophys Res Commun, 183(1), 258-264.
https://doi.org/10.1016/0006-291x(92)91637-6 Publication
Researcher Affiliations
- Institute of Industrial Chemistry, University of Padua, Italy.
MeSH Terms
- Amino Acid Sequence
- Animals
- Apoproteins / chemical synthesis
- Cytochrome c Group / chemical synthesis
- Cytochromes c
- Heme / metabolism
- Horses
- Isomerism
- Mitochondria, Heart / metabolism
- Molecular Sequence Data
- Myocardium / enzymology
- Peptide Fragments / chemical synthesis
- Protein Conformation
Citations
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