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Peptide Bonds02:43

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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Dieckmann cyclization is an intramolecular Claisen condensation of diesters. The reaction occurs in the presence of a base and generates a cyclic β-ketoester as the final product. Commonly, 1, 6 and 1, 7-diesters are preferred substrates for the reaction since the generated five, and six-membered cyclic β-keto esters are particularly more stable.
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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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Protein and Protein Structure02:15

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Cyclizing Disulfide-Rich Peptides Using Sortase A.

Akello J Agwa1, David J Craik2, Christina I Schroeder3

  • 1Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, Australia.

Methods in Molecular Biology (Clifton, N.J.)
|June 5, 2019
PubMed
Summary
This summary is machine-generated.

Sortase A (SrtA) enzyme from Staphylococcus aureus can now cyclize disulfide-rich peptides. This method, tailored for specific peptides, achieves yields of 40-50% cyclized product.

Keywords:
CyclizationCyclotideHead-to-tail cyclic peptideKalata B1MacrocyclePeptide ligationSemienzymaticSortase A

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Peptide Chemistry

Background:

  • Sortase A (SrtA) is a transpeptidase enzyme from Staphylococcus aureus.
  • SrtA facilitates site-specific covalent attachment of surface proteins to the bacterial cell wall.
  • The enzyme recognizes the LPXTG motif, cleaves it, and forms a thioester intermediate.

Purpose of the Study:

  • To explore the utility of Sortase A (SrtA) as a tool for peptide cyclization.
  • To develop a method for creating cyclic disulfide-rich peptides using SrtA.

Main Methods:

  • Utilizing Sortase A (SrtA) for site-specific peptide ligation.
  • Optimizing reaction conditions for individual disulfide-rich peptides.
  • Employing N-terminal polyglycine as a nucleophilic acceptor.

Main Results:

  • Demonstrated successful application of SrtA for disulfide-rich peptide cyclization.
  • Achieved yields of 40-50% for cyclized peptides under optimized conditions.
  • Highlighted the enzyme's versatility in peptide modification.

Conclusions:

  • Sortase A (SrtA) is an effective enzyme for the cyclization of disulfide-rich peptides.
  • Tailoring reaction conditions is crucial for optimizing yields.
  • This method offers a novel approach for peptide engineering and synthesis.