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Infrared reflection-absorption spect...

Cai, Peng.

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Infrared reflection-absorption spectroscopy (IRRAS) studies of pulmonary surfactant related peptides in lipid monolayers.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Infrared reflection-absorption spectroscopy (IRRAS) studies of pulmonary surfactant related peptides in lipid monolayers./
Author:	Cai, Peng.
Description:	141 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-09, Section: B, page: 4589.
Contained By:	Dissertation Abstracts International65-09B.
Subject:	Chemistry, Physical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3148776
ISBN:	0496078860

Infrared reflection-absorption spectroscopy (IRRAS) studies of pulmonary surfactant related peptides in lipid monolayers.
Cai, Peng.

Infrared reflection-absorption spectroscopy (IRRAS) studies of pulmonary surfactant related peptides in lipid monolayers. - 141 p.

Source: Dissertation Abstracts International, Volume: 65-09, Section: B, page: 4589.

Thesis (Ph.D.)--Rutgers The State University of New Jersey - Newark, 2004.

Pulmonary surfactant, a lipid/protein complex that lines the air/water interface in the mammalian lung, functions to reduce the work of breathing. Structure-function relationships of native surfactant protein and their peptide analogs are widely investigated to facilitate the design of therapeutic agents for respiratory distress syndrome (RDS) in premature infants and in the adult version of the disease (ARDS).

ISBN: 0496078860Subjects--Topical Terms:

560527
Chemistry, Physical.

Infrared reflection-absorption spectroscopy (IRRAS) studies of pulmonary surfactant related peptides in lipid monolayers.
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040 $a UnM $c UnM
100 1 $a Cai, Peng. $3 1933035
245 1 0 $a Infrared reflection-absorption spectroscopy (IRRAS) studies of pulmonary surfactant related peptides in lipid monolayers.
300 $a 141 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-09, Section: B, page: 4589.
500 $a Director: Richard Mendelsohn.
502 $a Thesis (Ph.D.)--Rutgers The State University of New Jersey - Newark, 2004.
520 $a Pulmonary surfactant, a lipid/protein complex that lines the air/water interface in the mammalian lung, functions to reduce the work of breathing. Structure-function relationships of native surfactant protein and their peptide analogs are widely investigated to facilitate the design of therapeutic agents for respiratory distress syndrome (RDS) in premature infants and in the adult version of the disease (ARDS).
520 $a The current studies used infrared reflection-absorption spectroscopy (IRRAS) to characterize surfactant protein related peptides and native porcine SP-C (Surfactant Protein C) directly in lipid monolayers. IRRAS is currently the only method able to provide molecular level information in situ at the air/water interface.
520 $a The first project of this thesis concerned the secondary structural transformation (helix ↔ sheet) of an isotopically labeled SP-B9--36 segment of SP-B (Surfactant Protein B) at the air/water interface. The amide bonds of selected residues were isotopically labeled with 13C = O, this approach enabled us to pinpoint the location within the sequence of the surface pressure induced conformational change in this peptide.
520 $a The second project is primarily aimed at the secondary structures/orientations of peptides used as therapeutic agents for RSD. The peptide sequences were based on model amphipathic helical motifs in the surfactant protein, SP-B. The secondary structures and orientations of KL4 (KLLLLKLLLLKLLLLKLLLLK) and L3K (LLKLLKLLLKLLKKLLKLLL) peptides were evaluated in lipid monolayers. The results provided an independent evaluation of lipid/peptide interaction in lipid monolayers and resolved a current controversy concerning the mechanism of action. The data show that the secondary structures adopted by these peptides in lipid monolayers are strongly dependent on lipid composition, charge, and surface pressure effects. A structural model is proposed for the response of the peptide to surface pressure changes.
520 $a The third project primarily addressed the molecular mechanism of surfactant respreading following compression. Recent high-resolution microscopy data have revealed the co-existence of monolayers and multilayers at high surface pressure. IRRAS was used to directly monitor the secondary structure and orientation of native, porcine SP-C in mixed monolayers and multilayers at air/water interface with DPPC, DPPG, and cholesterol. The results constitute the first quantitative measure of SP-C alpha-helical orientation in the mixed monolayer/multilayer domains at the air/water interface.
590 $a School code: 0461.
650 4 $a Chemistry, Physical. $3 560527
650 4 $a Biophysics, General. $3 1019105
690 $a 0494
690 $a 0786
710 2 0 $a Rutgers The State University of New Jersey - Newark. $3 1017745
773 0 $t Dissertation Abstracts International $g 65-09B.
790 1 0 $a Mendelsohn, Richard, $e advisor
790 $a 0461
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3148776