NDLI: Location of Structural Transitions in an Isotopically Labeled Lung Surfactant SP-B Peptide by IRRAS

Content Provider	PubMed Central
Author	Flach, Carol R. Cai, Peng Dieudonné, Darline Brauner, Joseph W. Keough, Kevin M. W. Stewart, June Mendelsohn, Richard
Copyright Year	2003
Abstract	Pulmonary surfactant, a lipid/protein complex that lines the air/water interface in the mammalian lung, functions to reduce the work of breathing. Surfactant protein B (SP-B) is a small, hydrophobic protein that is an essential component of this mixture. Structure-function relationships of SP-B are currently under investigation as the protein and its peptide analogs are being incorporated into surfactant replacement therapies. Knowledge of the structure of SP-B and its related peptides in bulk and monolayer phases will facilitate the design of later generation therapeutic agents. Prior infrared reflection-absorption spectroscopic studies reported notable, reversible surface pressure-induced antiparallel β-sheet formation in a synthetic peptide derived from human SP-B, residues 9–36 (SP-B9–36). In the current work, infrared reflection-absorption spectroscopy is applied in conjunction with isotopic labeling to detect the site and pressure dependence of the conformational change. SP-B9–36, synthesized with 13C=O-labeled Ala residues in positions 26, 28, 30, and 32, shifted the β-sheet marker band to ∼1600 cm−1 and thus immediately identified this structural element within the labeled region. Surface pressure-induced alterations in the relative intensities of Amide I band constituents are interpreted using a semiempirical transition dipole coupling model. In addition, electron micrographs reveal the formation of tubular myelin structures from in vitro preparations using SP-B9–36 in place of porcine SP-B indicating that the peptide has the potential to mimic this property of the native protein.
Starting Page	340
File Format	PDF
ISSN	15420086
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	1
Volume Number	85
Language	English
Publisher	Biophysical Society
Publisher Date	2003-07-01
Access Restriction	Open
Rights Holder	Biophysical Society
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Combinations of fluorescently labeled pulmonary surfactant proteins SP-B and SP-C in phospholipid films.

Lipid bilayer surface association of lung surfactant protein SP-B, amphipathic segment detected by flow immunofluorescence.

Reactive Oxygen Species Inactivation of Surfactant Involves Structural and Functional Alterations to Surfactant Proteins SP-B and SP-C

Effects of lung surfactant proteins, SP-B and SP-C, and palmitic acid on monolayer stability.

Lung Surfactant Protein A (SP-A) Interactions with Model Lung Surfactant Lipids and an SP-B Fragment

Lipid Polymorphism Induced by Surfactant Peptide SP-B1-25

Synchrotron X-ray study of lung surfactant-specific protein SP-B in lipid monolayers.

The Effect of a C-Terminal Peptide of Surfactant Protein B (SP-B) on Oriented Lipid Bilayers, Characterized by Solid-State 2H- and 31P-NMR

Surface pressure induced structural transitions of an amphiphilic peptide in pulmonary surfactant systems by an in situ PM-IRRAS study

Location of Structural Transitions in an Isotopically Labeled Lung Surfactant SP-B Peptide by IRRAS

Similar Documents

Combinations of fluorescently labeled pulmonary surfactant proteins SP-B and SP-C in phospholipid films.

Lipid bilayer surface association of lung surfactant protein SP-B, amphipathic segment detected by flow immunofluorescence.

Reactive Oxygen Species Inactivation of Surfactant Involves Structural and Functional Alterations to Surfactant Proteins SP-B and SP-C

Effects of lung surfactant proteins, SP-B and SP-C, and palmitic acid on monolayer stability.

Lung Surfactant Protein A (SP-A) Interactions with Model Lung Surfactant Lipids and an SP-B Fragment

Lipid Polymorphism Induced by Surfactant Peptide SP-B1-25

Synchrotron X-ray study of lung surfactant-specific protein SP-B in lipid monolayers.

The Effect of a C-Terminal Peptide of Surfactant Protein B (SP-B) on Oriented Lipid Bilayers, Characterized by Solid-State 2H- and 31P-NMR

Surface pressure induced structural transitions of an amphiphilic peptide in pulmonary surfactant systems by an in situ PM-IRRAS study

Location of Structural Transitions in an Isotopically Labeled Lung Surfactant SP-B Peptide by IRRAS