Determination of structure by Circular Dichroism (CD)
Avacta offer Circular Dichroim analysis as a stand alone fee-for-service or as part of a wider package of tailor made analytics to suit your needs. It is especially suitable for detecting structural changes in characterisation and comparability studies and its use is recommended in conjunction with FTIR or Raman spectroscopy.
Far UV CD
Circular dichroism has been widely applied to the study of protein secondary structure and various features in the CD spectra can be attributed to different conformations. Features in the far UV CD region (~190-240 nm) have been used to determine the relative proportions of each of the secondary structure elements (α-helix, β-sheet and random coil). In this region of the spectrum the signal originates in the peptide bonds of the protein. Far UV Circular dichroism will enable analysis of secondary structural changes in the monoclonal antibody protein and provide a key quality attribute test for the manufactured protein.
Near UV CD
Features in the near UV region (240-350 nm) have been reported to be sensitive to local tertiary structure around aromatic residues (tryptophan, tyrosine and phenylalanine) and disulphide bonds. Near UV CD spectra generates an effective fingerprint of the chiral environment of these aromatic residues, thus providing a tool to monitor their local conformation. Near UV circular dichroism will enable analysis of tertiary structural changes in the monoclonal antibody protein and could provide a quality attribute test for the manufactured protein.
Avacta facilities include the JASCO J-810 Spectropolarimeter for recording Circular Dichroism measurements.