Influence of metal ions on phosphatidylcholine-bovine serum albumin model membrane, an FTIR study
Influence of metal ions on phosphatidylcholine-bovine serum albumin model membrane, an FTIR study
Engineering Village 2
2006 Elsevier Inc.
Accession number: 063210057438
Title: Influence of metal ions on phosphatidylcholine-bovine serum albumin model membrane, an FTIR study
Authors: Wang, Fan; Yang, Zhanlan; Zhou, Yong; Weng, Shifu; Zhang, Li; Wu, Jinguang
Author affiliation: The State Key Laboratory of Rare Earth Materials Chemistry and Applications, College of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, China
Serial title: Journal of Molecular Structure
Abbreviated serial title: J. Mol. Struct.
Volume: v 794
Issue: n 1-3
Issue date: Aug 7 2006
Publication year: 2006
Pages: p 1-11
Language: English
ISSN: 0022-2860
CODEN: JMOSB4
Document type: Journal article (JA)
Publisher: Elsevier, Amsterdam, 1000 AE, Netherlands
Abstract: FTIR spectroscopy was used to study the interaction of K+, Ca2+ and Eu3+ ions and the Phosphatidylcholine (PC)-bovine serum albumin (BSA) complex. First, a PC-BSA interaction system was constructed. The analytical results of transmission electron microscope (TEM), quasi-elastic light scattering (QELS) techniques and FTIR-ATR spectroscopy indicated that PC molecules interacted with BSA in aqueous solutions. However, IR inspection was limited for aqueous solutions. Solid experimental condition was then employed, and FTIR spectra showed that the PC and BSA molecules incorporated with each other, which could represent their interactions in solutions. Then, the influence of metal ions on PC-BSA system was studied in solid experimental conditions, and FTIR spectroscopy was used in this study. The spectral results showed that: (1) K+, Ca2+ and Eu3+ ions all decreased the rigidities of acyl chains of PC in PC-BSA systems. (2) The interactions between Ca2+, Eu3+ ions and the hydrophilic phosphate ester and carbonyl ester groups of PC were stronger than that of K+ ions, while the influent modes of Ca2+ and Eu3+ ions on these regions were different. (3) When the relative molar content of Eu3+ ions to PC (Ri/p) reached 2, the coordination effect between Eu3+ ions and PO2- groups of PC was saturated. (4) The addition of these ions increased the content of a-helix structures of BSA, and decreased the content of ?-turn structures. By comparing these results with the interactions of K+, Ca2+, Eu3+ ions with phospholipid system in the absence of protein, some special characters were discovered in the acyl regions of PC, while their interactions results with the hydrophilic regions of PC were alike. It might be interpreted that these metal ions influenced the acyl chains of PC mediated from BSA molecules, and coordinated directly with the hydrophilic regions of PC. As for biological membrane was a system included both phospholipid and proteins, these characters suggested that phospholipid-protein mixture system could be a better model in the studies of interaction between metal ions and biological membranes using FTIR spectroscopy. ? 2006 Elsevier B.V. All rights reserved.
Number of references: 41
Ei main heading: Proteins
Ei controlled terms: Positive ions - Solutions - Esters - Hydrophilicity - Transmission electron microscopy - Light scattering
Uncontrolled terms: Phosphatidylcholine - Metal ions - Phosphate ester - Carbonyl ester groups
Ei classification codes: 804.1 Organic Compounds - 801 Chemistry - 931.2 Physical Properties of Gases, Liquids & Solids - 741.3 Optical Devices & Systems - 741.1 Light/Optics
Treatment: Theoretical (THR); Experimental (EXP)
DOI: 10.1016/j.molstruc.2006.01.021
Database: Compendex
Compilation and indexing terms, ? 2006 Elsevier Inc. All rights reserved
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