Adhesion forces of the blood plasma proteins on self-assembled monolayer surfaces of alkanethiolates with different functional groups measured by an atomic force microscope

被引:177
作者
Kidoaki, S [1 ]
Matsuda, T [1 ]
机构
[1] Natl Cardiovasc Ctr, Res Inst, Dept Bioengn, Suita, Osaka 5658565, Japan
关键词
D O I
10.1021/la990357k
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
To determine the adhesion force of representative blood plasma proteins (albumin (Alb), immunoglobulin G (IgG), and fibrinogen (Fib)) to foreign material surfaces, force-versus-distance curves were measured using an atomic force microscope (AFM) between the protein covalently immobilized AFM tips and the well-defined model surfaces of self-assembled monolayers (SAMs) of alkanethiolates terminated with different functional groups (CH3, NH2, OH, and COOH). From the f-d curves measured between the protein-immobilized tip and the SAM surface, the mechanical adhesion forces of the protein to the SAM surface (detachment force of protein from the surface) were determined. From the adhesion forces determined between the protein tip and the SAM surface and between like SAM-coated tips and surfaces (i.e., tip/surface combinations: CH3/CH3, NH2/NH2, OH/OH, and COOH/COOH),the thermodynamic adhesion strength (work of adhesion and surface pressure of SAM on a protein surface) was also determined according to the Dupre equation and Johnson, Kendall, and Roberts adhesion theory. The relative strength of thermodynamic adhesion of the proteins to the SAM surfaces was found with statistical significance to be in the following orders: (a) For Alb and IgG, CH3- much greater than (OH-, NH2-) > COOH-SAM surface; for Fib, CH3 much greater than) OH > NH2 > COOH. (b) On CH3-, NH2-, and OH-SAM surfaces, Fib exhibits higher adhesion than Alb and IgG.
引用
收藏
页码:7639 / 7646
页数:8
相关论文
共 45 条
[21]  
IVARSSON B, 1986, CRIT REV BIOCOMPAT, V2, P1
[22]   SURFACE ENERGY AND CONTACT OF ELASTIC SOLIDS [J].
JOHNSON, KL ;
KENDALL, K ;
ROBERTS, AD .
PROCEEDINGS OF THE ROYAL SOCIETY OF LONDON SERIES A-MATHEMATICAL AND PHYSICAL SCIENCES, 1971, 324 (1558) :301-&
[23]   SENSING DISCRETE STREPTAVIDIN BIOTIN INTERACTIONS WITH ATOMIC-FORCE MICROSCOPY [J].
LEE, GU ;
KIDWELL, DA ;
COLTON, RJ .
LANGMUIR, 1994, 10 (02) :354-357
[24]  
LUNDSTROM I, 1987, POLYM SURFACES INTER, V1, P201
[25]  
Macritchie F, 1978, Adv Protein Chem, V32, P283, DOI 10.1016/S0065-3233(08)60577-X
[26]   CRYSTALLOGRAPHIC REFINEMENT AND ATOMIC MODELS OF THE INTACT IMMUNOGLOBULIN MOLECULE KOL AND ITS ANTIGEN-BINDING FRAGMENT AT 3.0-A AND 1.9-A RESOLUTION [J].
MARQUART, M ;
DEISENHOFER, J ;
HUBER, R ;
PALM, W .
JOURNAL OF MOLECULAR BIOLOGY, 1980, 141 (04) :369-391
[27]   INTERMOLECULAR FORCES AND ENERGIES BETWEEN LIGANDS AND RECEPTORS [J].
MOY, VT ;
FLORIN, EL ;
GAUB, HE .
SCIENCE, 1994, 266 (5183) :257-259
[29]   CHEMICAL FORCE MICROSCOPY - EXPLOITING CHEMICALLY-MODIFIED TIPS TO QUANTIFY ADHESION, FRICTION, AND FUNCTIONAL-GROUP DISTRIBUTIONS IN MOLECULAR ASSEMBLIES [J].
NOY, A ;
FRISBIE, CD ;
ROZSNYAI, LF ;
WRIGHTON, MS ;
LIEBER, CM .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1995, 117 (30) :7943-7951
[30]   Structural activity of a cloned potassium channel (ROMK1) monitored with the atomic force microscope: The ''molecular-sandwich'' technique [J].
Oberleithner, H ;
Schneider, SW ;
Henderson, RM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (25) :14144-14149