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Probing nanoscale adhesion and structure at soft interfaces Ritchie, Kenneth Patrick
Abstract
Physical measurement at soft interfaces presents special problems. The compliance of the interface makes positional accuracy of secondary importance to force sensitivity. Only minuscule forces are required to displace a soft surface or to slowly overcome a small energetic barrier in an aqueous environment. The thesis is organized according to three aspects of measurement at soft interfaces and the parts are labelled by Roman numerals I—III. Each of these parts (I—III) contains results conclusions and discussions specific to the particular topic of the segment. I) To test adhesion and probe compliance at soft interfaces, the developement of a general, ultra-sensitive force measurement technique is described. The technique exploits a tunable force transducer comprised of a biomembrane capsule held under tension chemically bonded to a glass microsphere probe. The technique has a high sensitivity (in the range of pico- to nano-Newtons) and a large span of force loading rates. II) To demonstrate nanoscale mechanical testing of interfacial compliance, the ultrasensitive force probe was used to determine the thickness compressibility of the human red blood cell membrane. The membrane was found to be 100-fold softer than an ideal rubber. The minimum thickness of the red cell membrane was 58 ± 4 nm. This thickness implies that there are large proteins associated with the membrane that act to expand the tethered spectrin network. III) To demonstrate nanoscale testing of molecular adhesive strength, the probe has been used to rupture single receptor-ligand bonds (avidin-biotin). Recognizing that thermal activation underlies dissociation of weak bonds, a theory for the force-driven failure of point physical bonds is presented. The predictions from theory are verified by Brownian dynamics simulation. Bond failure is a kinetic process. The experimentally measured strength of the bond depends on the rate which force is applied to the linkage. A universal logarithmic rate dependence regime reveals information about the underlying bonding potential along the force-driven reaction pathway. The form of the strength over a spectrum of loading rates gives the position and height of major energetic barriers along the bond failure pathway. Complex bonding potentials can thus be partially reconstructed and compared to the structures of the bonding species, if available.
Item Metadata
Title |
Probing nanoscale adhesion and structure at soft interfaces
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Creator | |
Publisher |
University of British Columbia
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Date Issued |
1998
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Description |
Physical measurement at soft interfaces presents special problems. The compliance of the
interface makes positional accuracy of secondary importance to force sensitivity. Only
minuscule forces are required to displace a soft surface or to slowly overcome a small
energetic barrier in an aqueous environment. The thesis is organized according to three
aspects of measurement at soft interfaces and the parts are labelled by Roman numerals
I—III. Each of these parts (I—III) contains results conclusions and discussions specific to
the particular topic of the segment.
I) To test adhesion and probe compliance at soft interfaces, the developement of a
general, ultra-sensitive force measurement technique is described. The technique exploits
a tunable force transducer comprised of a biomembrane capsule held under tension chemically
bonded to a glass microsphere probe. The technique has a high sensitivity (in the
range of pico- to nano-Newtons) and a large span of force loading rates.
II) To demonstrate nanoscale mechanical testing of interfacial compliance, the ultrasensitive
force probe was used to determine the thickness compressibility of the human
red blood cell membrane. The membrane was found to be 100-fold softer than an ideal
rubber. The minimum thickness of the red cell membrane was 58 ± 4 nm. This thickness
implies that there are large proteins associated with the membrane that act to expand
the tethered spectrin network.
III) To demonstrate nanoscale testing of molecular adhesive strength, the probe has
been used to rupture single receptor-ligand bonds (avidin-biotin). Recognizing that thermal
activation underlies dissociation of weak bonds, a theory for the force-driven failure
of point physical bonds is presented. The predictions from theory are verified by Brownian
dynamics simulation. Bond failure is a kinetic process. The experimentally measured
strength of the bond depends on the rate which force is applied to the linkage. A universal
logarithmic rate dependence regime reveals information about the underlying bonding
potential along the force-driven reaction pathway. The form of the strength over a spectrum
of loading rates gives the position and height of major energetic barriers along the
bond failure pathway. Complex bonding potentials can thus be partially reconstructed
and compared to the structures of the bonding species, if available.
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Extent |
6422136 bytes
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Genre | |
Type | |
File Format |
application/pdf
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Language |
eng
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Date Available |
2009-06-25
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Provider |
Vancouver : University of British Columbia Library
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Rights |
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.
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DOI |
10.14288/1.0085691
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URI | |
Degree | |
Program | |
Affiliation | |
Degree Grantor |
University of British Columbia
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Graduation Date |
1998-11
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Campus | |
Scholarly Level |
Graduate
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Aggregated Source Repository |
DSpace
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Item Media
Item Citations and Data
Rights
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.