Matches in UGent Biblio for { <https://biblio.ugent.be/publication/3193646#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B605440.
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- aggregation date "2012".
- aggregation format "application/pdf".
- aggregation hasFormat 3193646.bibtex.
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- aggregation isPartOf urn:issn:0003-2700.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Near-infrared spectroscopy for in-line monitoring of protein unfolding and its interactions with lyoprotectants during freeze-drying".
- aggregation abstract "This work presents near-infrared spectroscopy (NIRS) as an in-line process analyzer for monitoring protein unfolding and protein-lyoprotectant hydrogen bond interactions during freeze-drying. By implementing a noncontact NIR probe in the freeze-drying chamber, spectra of formulations containing a model protein immunoglobulin G (IgG) were collected each process minute. When sublimation was completed in the cake region illuminated by the NIR probe, the frequency of the amide A/II band (near 4850 cm(-1)) was monitored as a function of water elimination. These two features were well correlated during protein dehydration in the absence of protein unfolding (desired process course), whereas consistent deviations from this trend to higher amide A/II frequencies were shown to be related to protein unfolding. In formulations with increased sucrose concentrations, the markedly decreased amide A/II frequencies seen immediately after sublimation indicated an increased extent. of hydrogen bond interaction between the protein's backbone and surrounding molecules. At the end of drying, there was evidence of nearly complete water substitution for formulations with 1%, 5%, and 10% sucrose. The presented approach shows promising perspectives for early fault detection of protein unfolding and for obtaining mechanistic process information on actions of lyoprotectants.".
- aggregation authorList BK961288.
- aggregation endPage "955".
- aggregation issue "2".
- aggregation startPage "947".
- aggregation volume "84".
- aggregation aggregates 3193664.
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