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Investigation of the Differences in Thermal Stability of Two Recombinant Human Serum Albumins with 1,2-Dipalmitoyl-Sn-Glycero-3-Phosphocholine Liposomes by U/V Circular Dichroism Spectropolarimetry.
MedLine Citation:
PMID:  22423959     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Previous studies have demonstrated that liposome - protein interactions can result in changes to the thermal stability of the protein. We utilized far U/V circular dichroism spectropolarimetry and fluorescence spectroscopy to investigate the interaction of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) liposomes with two recombinant human serum albumins (rHSA). We demonstrate that rHSA expressed in Oryza sativa (OsrHSA) has improved secondary structure thermal stability compared to rHSA expressed in Pichia pastoris (PprHSA). A similar stability profile was observed when comparing bovine serum albumin (BSA) and defatted bovine serum albumin (dfBSA), suggesting the presence of fatty acids may be responsible for the improved stability of OsrHSA. Addition of DPPC liposomes reduced the thermal stability of both OsrHSA and BSA, but not of PprHSA or dfBSA. DPPC liposomes may disrupt stabilizing native fatty acids on OsrHSA and BSA.
Authors:
Grant Frahm; Terry Donald Cyr; Daryl G S Smith; Lisa Walrond; Michael J W Johnston
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-3-16
Journal Detail:
Title:  The journal of physical chemistry. B     Volume:  -     ISSN:  1520-5207     ISO Abbreviation:  -     Publication Date:  2012 Mar 
Date Detail:
Created Date:  2012-3-19     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101157530     Medline TA:  J Phys Chem B     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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