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FT-IR spectroscopy and scanning prob...

Brockman, Jennifer Michelle Wilkin.

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FT-IR spectroscopy and scanning probe microscopy of organic thin films with applications to pulmonary surfactant.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	FT-IR spectroscopy and scanning probe microscopy of organic thin films with applications to pulmonary surfactant./
Author:	Brockman, Jennifer Michelle Wilkin.
Description:	218 p.
Notes:	Director: Richard A. Dluhy.
Contained By:	Dissertation Abstracts International59-04B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9828369
ISBN:	059180929X

FT-IR spectroscopy and scanning probe microscopy of organic thin films with applications to pulmonary surfactant.
Brockman, Jennifer Michelle Wilkin.

FT-IR spectroscopy and scanning probe microscopy of organic thin films with applications to pulmonary surfactant. - 218 p.

Director: Richard A. Dluhy.

Thesis (Ph.D.)--University of Georgia, 1998.

Monolayer and bilayer films composed of lipids and proteins are critical to the field of biophysics as they often serve as membrane mimetic models and are constructed to model mammalian pulmonary surfactant. Pulmonary surfactant, a complex mixture of lipids and proteins, exists as a monomolecular film at the air-alveolar interface in the lung and reduces the surface tension at this interface to near zero values. This allows for efficient gas exchange at the interface and prevents the collapse of the lung alveoli during successive breathing cycles.

ISBN: 059180929XSubjects--Topical Terms:

1019105
Biophysics, General.

FT-IR spectroscopy and scanning probe microscopy of organic thin films with applications to pulmonary surfactant.
LDR:03403nam 2200301 a 45 001 932627
005 20110505
008 110505s1998 eng d
020 $a 059180929X
035 $a (UnM)AAI9828369
035 $a AAI9828369
040 $a UnM $c UnM
100 1 $a Brockman, Jennifer Michelle Wilkin. $3 1256368
245 1 0 $a FT-IR spectroscopy and scanning probe microscopy of organic thin films with applications to pulmonary surfactant.
300 $a 218 p.
500 $a Director: Richard A. Dluhy.
500 $a Source: Dissertation Abstracts International, Volume: 59-04, Section: B, page: 1616.
502 $a Thesis (Ph.D.)--University of Georgia, 1998.
520 $a Monolayer and bilayer films composed of lipids and proteins are critical to the field of biophysics as they often serve as membrane mimetic models and are constructed to model mammalian pulmonary surfactant. Pulmonary surfactant, a complex mixture of lipids and proteins, exists as a monomolecular film at the air-alveolar interface in the lung and reduces the surface tension at this interface to near zero values. This allows for efficient gas exchange at the interface and prevents the collapse of the lung alveoli during successive breathing cycles.
520 $a In the current work, infrared spectroscopy and atomic force microscopy were used to probe phospholipid binary mixtures and phospholipid-protein ternary mixtures chosen as models for pulmonary surfactant. Films were studied in one of two basic ways: either in-situ at the air-water interface, or after transfer to solid substrates for subsequent, ex-situ analysis. Results from a combined ATR/$\sp{31} $p NMR method indicate that the rate at which binary mixtures of DPPC-d$\sb{62}$ and DOPG are compressed at the air-water interface affects the fractional composition of the phospholipid components that are subsequently transferred to germanium internal reflection elements. Atomic force microscopy was employed to probe the surface topographies of phospholipid monolayer films that had undergone a variety of compression and expansion conditions before transfer to mica substrates, and showed that increased compression rates decreased the molecular packing efficiency in the films and resulted in "flaws" in the monolayer surface.
520 $a Infrared reflectance-absorption spectroscopy at the air-water interface was used to study, in-situ, the squeeze-out of unsaturated phospholipid components from mixed monolayer films of phosphocholine and phosphoglycerol and to monitor the effects of surfactant proteins SP-B and SP-C on the phospholipid acyl chain conformations in similar model mixtures. Results, which confirmed the squeeze-out hypothesis of surfactant function, showed that significant populations unsaturated lipids were excluded from these films upon compression whereas saturated lipids were not. Analysis of spectral band parameters suggests that the surfactant proteins affect the PC and PG lipids differently. The proteins had a significant condensing effect on the phosphoglycerol components in the films but appeared to influence the phosphocholine component of the mixed films very little.
590 $a School code: 0077.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Analytical. $3 586156
690 $a 0486
690 $a 0786
710 2 0 $a University of Georgia. $3 515076
773 0 $t Dissertation Abstracts International $g 59-04B.
790 $a 0077
790 1 0 $a Dluhy, Richard A., $e advisor
791 $a Ph.D.
792 $a 1998
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9828369