PM-IRRAS investigation of the interaction of serum albumin and fibrinogen with a biomedical-grade stainless steel 316LVM surface

被引：40
作者：
Desroches, Marie J. [1 ]
Chaudhary, Nida [1 ]
Omanovic, Sasha [1 ]
机构：
[1] McGill Univ, Dept Chem Engn, Montreal, PQ H3A 2B2, Canada
来源：
BIOMACROMOLECULES | 2007年 / 8卷 / 09期
关键词：
D O I：
10.1021/bm070289d
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) was applied to investigate the interaction of bovine serum albumin (BSA) and fibrinogen with a biomedical-grade 316LVM stainless steel surface, in terms of the adsorption thermodynamics and adsorption-induced secondary structure changes of the proteins. Highly negative apparent Gibbs energy of adsorption values revealed a spontaneous adsorption of both proteins onto the surface, accompanied by significant changes in their secondary structure. It was determined that, at saturated surface coverages, lateral interactions between the adsorbed BSA molecules induced rather extensive secondary structure changes. Fibrinogen's two coiled coils appeared to undergo negligible secondary structure changes upon adsorption of the protein, while large structural rearrangements of the protein's globular domains occurred upon adsorption. The secondary structure of adsorbed fibrinogen was not influenced by lateral interactions between the adsorbed fibrinogen molecules. PM-IRRAS was deemed to be viable for investigating protein adsorption and for obtaining information on adsorption-induced changes in their secondary structures.
引用
收藏
页码：2836 / 2844
页数：9
相关论文
共 89 条
  • [1] Interfacial adsorption of fibrinogen and its inhibition by RGD peptide: a combined physical study
    Armstrong, J
    Salacinski, HJ
    Mu, QS
    Seifalian, AM
    Peel, L
    Freeman, N
    Holt, CM
    Lu, JR
    [J]. JOURNAL OF PHYSICS-CONDENSED MATTER, 2004, 16 (26) : S2483 - S2491
  • [2] SPECTROSCOPIC STUDIES OF FIBRINOGEN AND ITS PLASMIN-DERIVED FRAGMENTS
    AZPIAZU, I
    CHAPMAN, D
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1992, 1119 (03) : 268 - 274
  • [3] Bailly AL, 1996, J BIOMED MATER RES, V30, P101, DOI 10.1002/(SICI)1097-4636(199601)30:1<101::AID-JBM13>3.0.CO
  • [4] 2-R
  • [5] Adsorption of fibrinogen onto macroporous, biocompatible sponges based on poly(2-hydroxyethyl methacrylate)
    Bajpai, A. K.
    Mishra, D. D.
    [J]. JOURNAL OF APPLIED POLYMER SCIENCE, 2006, 102 (02) : 1341 - 1355
  • [6] FTIR-ATR and radiolabeling study of structural modifications during protein adsorption on hydrophilic surfaces.: 2.: The Case of apo-α-lactalbumine
    Bentaleb, A
    Abele, A
    Haikel, Y
    Schaaf, P
    Voegel, JC
    [J]. LANGMUIR, 1999, 15 (14) : 4930 - 4933
  • [7] Adsorption-induced conformational changes of proteins onto ceramic particles: Differential scanning calorimetry and FTIR analysis
    Brandes, Natascha
    Welzel, Petra B.
    Werner, Carsten
    Kroh, Lothar W.
    [J]. JOURNAL OF COLLOID AND INTERFACE SCIENCE, 2006, 299 (01) : 56 - 69
  • [8] BRASH JL, 1993, J BIOMAT SCI-POLYM E, V4, P591, DOI 10.1163/156856293X00816
  • [9] Electrochemical quartz crystal nanobalance (EQCN) studies of the adsorption behaviour of an enzyme, mandelate racemase, and its substrate, mandelic acid, on Pt
    Brosseau, CL
    St Maurice, M
    Bearne, SL
    Roscoe, SG
    [J]. ELECTROCHIMICA ACTA, 2005, 50 (06) : 1289 - 1297
  • [10] The crystal structure of modified bovine fibrinogen
    Brown, JH
    Volkmann, N
    Jun, G
    Henschen-Edman, AH
    Cohen, C
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (01) : 85 - 90
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