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Peptide backbone modifications on the C-terminal hexapeptide of neurotensin

Jürgen Einsiedel1, Harald Hübner, Maud Hervet

  • 1Department of Chemistry and Pharmacy, Emil Fischer Center, Friedrich Alexander University, D-91052 Erlangen, Germany.

Bioorganic & Medicinal Chemistry Letters
|February 16, 2008
PubMed

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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