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Instruments / Technical Area	Publication Details	Published	Actions
B23-Circular Dichroism	Application of circular dichroism and magnetic circular dichroism for assessing biopharmaceuticals formulations photo-stability and small ligands binding properties Edoardo Longo , Rohanah Hussain , Giuliano Siligardi International Journal Of Pharmaceutics 480, 84 - 91 DOI: 10.1016/j.ijpharm.2015.01.026 PMID: 25596417 Diamond Proposal Number(s): [7559, 8714, 9786, 10484] Open Access Show Abstract ▼ Abstract: Synchrotron radiation circular dichroism (SRCD) is a powerful tool for photo-stability assessment of proteins. Recently our research has been interested in applying SRCD to develop screening methodologies for accelerated photo-stability assessment of monoclonal antibody formulations. Despite it was proven to be reliable and applicable within a wide range of salts and excipients containing solutions, the presence of far-UV (<260 nm) strong absorbing species (e.g., sodium chloride, histidine, arginine) in common formulations completely prevent the analysis. Herein, we propose a new method based on CD coupled with magnetic CD (MCD) to address the problem and offer an additional versatile tool for monitoring the photo-stability. This is done by assessing the stability of the samples by looking at the near-UV band, as well as giving insights in the denaturation mechanism. We applied this method to four mAbs formulations and correlated the results with dynamic light scattering data. Finally, we applied MCD in ligand interaction to key proteins such as lysozyme, comparing the human with the hen enzyme in the binding of N,N′,N′′-triacetylchitotriose.	Mar 2015
B23-Circular Dichroism	The effect of palmitoylation on the conformation and physical stability of a model peptide hormone Edoardo Longo , Emiliana De Santis , Rohanah Hussain , Chris Van Der Walle , Jose Casas-finet , Shahid Uddin , Ana Dos Santos , Giuliano Siligardi International Journal Of Pharmaceutics 472, 156 - 164 DOI: 10.1016/j.ijpharm.2014.06.008 PMID: 24928136 Diamond Proposal Number(s): [7559, 8082] Show Abstract ▼ Abstract: Peptides are ideal drug candidates due to their potency and specificity, but suffer from a short half-life and low membrane permeability. Acylation can overcome these limitations but the consequences to stability under different formulation conditions and stresses are largely unreported. Using synchrotron radiation circular dichroism (SRCD), we show that palmitoylation of a 28 amino acid peptide hormone (pI 9.82) induced a structural transition from 310-helix to α-helix, irrespective of buffer type and pH investigated (5.5–8.0) when compared to the non acylated analogues. These conformational preferences were retained in the presence of non-ionic micelles but not anionic micelles, which induced an α-helical structure for all peptides. Palmitoylation promoted an irreversible peptide denaturation under thermal stress at pH ≥ 6.5 and increased the propensity for loss of helical structure under high photon flux (here used as a novel accelerated photostability test). The presence of either ionic or non-ionic micelles did not recover these conformational changes over the same irradiation period. These results demonstrate that acylation can change peptide conformation and decrease thermal-/photo-stability, with important consequences for drug-development strategies.	Sep 2014

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