Biomedical Engineering Reference
In-Depth Information
Heart and Vascular Diseases,
National Heart, Lung, and Blood
Institute, NIH Publication
No. 85-2185, revised July 1985, U.S.
Department of Health and Human
Services.
Miles, M.J., McMaster, T., Carr, H.J.,
Tatham, A.S., Shewry, P.R., Field, J.M.,
Belton, P.S., Jeenes, D., Hanley, B.,
Whittam, M., Cairns, P., Morris, V.J.,
and Lambert, N. (1990). Scanning
tunneling microscopy of biomolecules.
J. Vac. Sci. Technol. A 8: 698-702.
Neumann, A.W., Absolom, D.R., Francis,
D.W., Omenyi, S.N., Spelt, J.K.,
Policova, Z., Thomson, C., Zingg, W.,
and Van Oss, C.J. (1983).
Measurement of surface tensions of
blood cells and proteins. Ann. N.Y.
Acad. Sci. 416: 276-298.
Quate, C.F. (1997). Scanning probes as
a lithography tool for nanostructures.
Surf. Sci. 386: 259-264.
Ratner, B.D. (1983). Analysis of surface
contaminants on intraocular lenses.
Arch. Ophthal. 101: 1434-1438.
Ratner, B.D. (1988). Surface
Characterization of Biomaterials.
Elsevier, Amsterdam.
Ratner, B.D., and Castner, D.G. (1997).
Electron spectroscopy for chemical
analysis. in Surface Analysis d The
Principal Techniques. J.C. Vickerman,
ed. John Wiley and Sons, Ltd.,
Chichester, UK, pp. 43-98.
Ratner, B.D., and McElroy, B.J. (1986).
Electron spectroscopy for chemical
analysis: applications in the biomedical
sciences. in Spectroscopy in the
Biomedical Sciences, R.M. Gendreau,
ed. CRC Press, Boca Raton, FL,
pp. 107-140.
Rugar, D., and Hansma, P. (1990). Atomic
force microscopy. Physics Today 43:
23-30.
Scheutzle, D., Riley, T.L., deVries, J.E., and
Prater, T.J. (1984). Applications of
high-performance mass spectrometry to
the surface analysis of materials. Mass
Spectrom. 3: 527-585.
Shen, Y.R. (1989). Surface properties
probed by second-harmonic and
sum-frequency generation. Nature
337(6207): 519-525.
Somorjai, G.A. (1981). Chemistry in Two
Dimensions: Surfaces. Cornell Univ.
Press, Ithaca, NY.
Somorjai, G.A. (1994). Introduction to
Surface Chemistry and Catalysis. John
Wiley and Sons, New York.
Storey, J.M.E., Barber, T.E., Shelton, R.D.,
Wachter, E.A., Carron, K.T., and Jiang,
Y. (1995). Applications of surface-
enhanced Raman scattering (SERS) to
chemical detection. Spectroscopy 10(3):
20-25.
Tirrell, M., Kokkoli, E., and Biesalski, M.
(2000). The role of surface science in
bioengineered materials. Surf. Sci. 500:
61-83.
Urban, M.W. (1993). Vibrational
Spectroscopy of Molecules and
Macromolecules on Surfaces . Wiley-
Interscience, New York.
Van Vaeck, L., Adriaens, A., and Gijbels, R.
(1999). Static secondary ion mass
spectrometry (S-SIMS): part I.
Methodology and structural
interpretation. Mass Spectrom. Rev.
18: 1d47.
Vickerman, J.C. (1997). Surface Analysis:
The Principal Techniques. John Wiley
and Sons, Chichester, UK.
Vickerman, J.C., Brown, A., and Reed, N.
M. (1989). Secondary Ion Mass
Spectrometry, Principles and
Applications. Clarendon Press, Oxford.
Wagner, M.S., and Castner, D.G. (2001).
Characterization of adsorbed protein
films by time-of-flight secondary ion
mass spectrometry with principal
component analysis. Langmuir 17:
4649-4660.
Wagner, M.S., McArthur, S.L., Shen, M.,
Horbett, T.A., and Castner, D.G.
(2002). Limits of detection for time of
flight secondary ion mass spectrometry
(ToF-SIMS) and X-ray photo-electron
spectroscopy (XPS): detection of low
amounts of adsorbed protein. J.
Biomater. Sci. Polymer Ed. 13(4):
407-428.
Watts, J.F., and Wolstenholme, J. (2003).
An Introduction to Surface Analysis by
XPS and AES. John Wiley & Sons,
Chichester, UK.
Wilson, D.L., Martin, R., Hong, S.I.,
Cronin-Golomb, M., Mirkin, C.A., and
Kaplan, D.L. (2001). Surface
organization and nanopat-terning of
collagen by dip-pen nanolithography.
Proc. Natl. Acad. Sci. USA 98(24):
13,360-13,664.
Zisman, W.A. (1964). Relation of the
equilibrium contact angle to liquid and
solid constitution. in Contact Angle,
Wettability and Adhesion, ACS
Advances in Chemistry Series , Vol. 43,
F.M. Fowkes, ed. American Chemical
Society, Washington, D.C., pp. 1-51.
neutral carrier system for biochemical processes, how-
ever. Far from this, water is an active participant in
biology, which simply could not and would not work
the way it does without the special mediating proper-
ties of water. Moreover, it is widely believed that water
is the first molecule to contact biomaterials in any
clinical application ( Andrade et al. , 1981; Baier, 1978 ).
This is because water is the majority molecule in any
biological mixture, constituting 70 wt% or more of
most living organisms, and because water is such a small
and agile molecule, only about 0.25 nm in the longest
dimension. Consequently, behavior of water near sur-
faces and the role of water in biology are very important
subjects in biomaterials science. Some of these impor-
tant aspects of water are discussed here.
3.1.5 Role of water
in biomaterials
Erwin A. Vogler
The primary role water plays in biomaterials is as
a solvent system. Water, the ''universal ether'' ( Baier
and Meyer, 1996 ), dissolves inorganic salts and large
organic macromolecules such as proteins or carbohy-
drates (solutes) with nearly equal efficiency ( Pain,
1982 ). Water suspends living cells, as in blood, for ex-
ample, and is the principal constituent of the interstitial
fluid that bathes tissues. Water is not just a bland,
Search WWH ::




Custom Search