Investigation of the Differences in Thermal Stability of Two Recombinant Human Serum Albumins with 1,2-Dipalmitoyl-sn-glycero-3-phosphocholine Liposomes by UV Circular Dichroism Spectropolarime
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- 作者：Grant E. Frahm ; Terry D. Cyr ; Daryl G. S. Smith ; Lisa D. Walrond ; Michael J. W. Johnston
- 刊名：The Journal of Physical Chemistry B
- 出版年：2012
- 出版时间：April 19, 2012
- 年：2012
- 卷：116
- 期：15
- 页码：4661-4670
- 全文大小：529K
- 年卷期：v.116,no.15(April 19, 2012)
- ISSN：1520-5207
文摘
Previous studies have demonstrated that liposome鈥損rotein interactions can result in changes to the thermal stability of the protein. We utilized far-UV circular dichroism spectropolarimetry and fluorescence spectroscopy to investigate the interaction of 1,2-dipalmitoyl-<i>sni>-glycero-3-phosphocholine (DPPC) liposomes with two recombinant human serum albumins (rHSA). We demonstrate that rHSA expressed in <i>Oryza sativai> (OsrHSA) has improved secondary structure thermal stability compared to rHSA expressed in <i>Pichia pastorisi> (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.