Structure and properties of phospholipid–peptide monolayers containing monomeric SP-B1–25

Shanmukh, Saratchandra; Biswas, Nilanjana; Waring, Alan J.; Walther, Frans J.; Wang, Zhendong; Chang, Yusuo; Notter, Robert H.; Dluhy, Richard A.

doi:10.1016/j.bpc.2004.09.009

Cited by 33 publications

(26 citation statements)

References 45 publications

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“…The lipid mixture, used to formulate the synthetic peptides, was based on the known composition of calf lung surfactant lipids (13) and contained (in mg/ml) 16 DPPC, 10 DOPC, 3 POPG, 1 POPE, 3 POPS, and 2 cholesterol, or a total of 35 mg lipids/ml in 150 mM phosphate buffer saline solution (pH 7.0) (59). The lipid mixture alone was used as a negative control.…”

Section: Methodsmentioning

confidence: 99%

“…7C). Polarization modulation infrared reflectance absorption spectroscopy of the SP-B 1-25 peptide in 4:1 DPPC:DOPG monolayers shows a reorientation of the peptide from parallel to perpendicular with respect to the interface at high compression (59), placing the peptide in a configuration that would support extrusion of discoid bicelles. Moreover, the amphipathic helix region of SP-B, estimated to span at least 8 amino acids (residues 14 -21) (38), is ϳ12 Å in length while the lipid tail region in the bilayer spans ϳ20 Å (73), suggesting that two helices could comfortably span the length of the tail region of the bilayer as outlined in Fig.…”

Section: L343 Importance Of Sp-b Nh2-terminal Insertion Sequencementioning

confidence: 99%

“…While there are no high-resolution crystal or NMR structures of the native SP-B protein, the structure of the NH 2 terminus up to residue 25 is well defined as determined by a combination of NMR, FTIR, and Raman spectroscopy (6,22,38,53,59,71). Residues 1-9 (FPIPLPYCW), proposed to act as an "insertion sequence," comprise a hydrophobic region containing a poly-proline-like sequence.…”

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confidence: 99%

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Functional importance of the NH₂-terminal insertion sequence of lung surfactant protein B

Frey

Pocivavsek

Waring

et al. 2010

American Journal of Physiology-Lung Cellular and Molecular Phys

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Lung surfactant protein B (SP-B) is required for proper surface activity of pulmonary surfactant. In model lung surfactant lipid systems composed of saturated and unsaturated lipids, the unsaturated lipids are removed from the film at high compression. It is thought that SP-B helps anchor these lipids closely to the monolayer in three-dimensional cylindrical structures termed "nanosilos" seen by atomic force microscopy imaging of deposited monolayers at high surface pressures. Here we explore the role of the SP-B NH2 terminus in the formation and stability of these cylindrical structures, specifically the distribution of lipid stack height, width, and density with four SP-B truncation peptides: SP-B 1-25, SP-B 9 -25, SP-B 11-25, and SP-B 1-25Nflex (prolines 2 and 4 substituted with alanine). The first nine amino acids, termed the insertion sequence and the interface seeking tryptophan residue 9, are shown to stabilize the formation of nanosilos while an increase in the insertion sequence flexibility (SP-B 1-25Nflex) may improve peptide functionality. This provides a functional understanding of the insertion sequence beyond anchoring the protein to the two-dimensional membrane lining the lung, as it also stabilizes formation of nanosilos, creating reversible repositories for fluid lipids at high compression. In lavaged, surfactant-deficient rats, instillation of a mixture of SP-B 1-25 (as a monomer or dimer) and synthetic lung lavage lipids quickly improved oxygenation and dynamic compliance, whereas SP-B 11-25 surfactants showed oxygenation and dynamic compliance values similar to that of lipids alone, demonstrating a positive correlation between formation of stable, but reversible, nanosilos and in vivo efficacy.

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Section: Methodsmentioning

confidence: 99%

Section: L343 Importance Of Sp-b Nh2-terminal Insertion Sequencementioning

confidence: 99%

mentioning

confidence: 99%

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Functional importance of the NH₂-terminal insertion sequence of lung surfactant protein B

Frey

Pocivavsek

Waring

et al. 2010

American Journal of Physiology-Lung Cellular and Molecular Phys

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“…[22,23] The interfacial behaviour of a monomeric human sequence of the pulmonary surfactant protein B, SP-B , parallels the behaviour of many peptides in solution, as observed by Shanmukh et al with polarization-modulated IRRAS. [24] When there is only a small amount of the peptide inside mixed lipid/peptide monolayers, the peptide is a-helical, while at higher peptide molar fraction it aggregates into b-sheets. The binding of Ras proteins through a membrane anchor [25] and the interaction of neuropeptide Y with lipid monolayers [26] have been investigated, and no secondary structure change was found.…”

Section: Introductionmentioning

confidence: 99%

Interactions of KLA Amphipathic Model Peptides with Lipid Monolayers

Erbe¹,

Kerth²,

Dathe³

et al. 2009

ChemBioChem

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Interactions of the cationic amphipathic peptide KLALKLALKALKAALKLA-NH(2) (KLAL) and its double D-amino acid replacement analogues l(11)k(12)-KLAL and k(9)a(10)-KLAL with lipid monolayers of anionic POPG, zwitterionic POPC and mixtures thereof at the air/water interface were investigated by infrared reflection- absorption spectroscopy (IRRAS). At high surface pressure (>30 mN m(-1)) all peptides incorporated into lipid monolayers containing at least 25 % anionic POPG, and adopted an alpha-helical conformation. Creation of free surface by expansion of the monolayers resulted in an additional adsorption of peptides from the subphase, but now in a beta-sheet conformation; this led to the coexistence of peptides in two distinctly different conformations within the lipid monolayer. The beta-sheets bound to the free surface could be squeezed out of the film by compressing the film to low surface areas, whereas the alpha-helices remained bound to the lipids until the film collapsed. When bound to the lipid monolayer, the helical axis of the peptides is oriented almost parallel to the surface of the monolayer.

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“…256 -261 The conformation and orientation of synthetic monomeric human-sequence SP-B 1 -25 (mSP-B 1 -25 was studied in films with phospholipids at the A/W interface by PM-IRRAS as a function of surface pressure and protein concentration. 262 k -correlation analysis was applied to the PM-IRRAS spectra to define changes in the secondary structure and rates of reorientation of mSP-B 1 -25 in the monolayer during compression. Analysis of the k -correlation plot in Fig.…”

Section: Study Of Protein Secondary Structure In Lipid Mixturesmentioning

confidence: 99%

The application of two‐dimensional correlation spectroscopy to surface and interfacial analysis

Dluhy

Shanmukh

Morita

2006

Surface & Interface Analysis

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Generalized two-dimensional correlation spectroscopy (2D COS) is a modern analytical tool that is increasingly being used in the interpretation of complex spectra that have broad, multiply overlapped spectral features. Besides functioning as a spectral resolution-enhancement tool similar to curvefitting or deconvolution, 2D COS possesses an additional advantage in that it is capable of discerning temporal relationships between intensity variations within a set of spectra. Infrared reflection-absorbance spectroscopy (IRRAS) at the air-water interface has been a very useful technique in studying the structure of biologically relevant molecules and the interaction between components of biological membranes in an environment close to what is found in nature. To better understand interfacial bio-mimetic structure, 2D COS can be applied to the IRRAS spectra to analyze changes in infrared intensities as a function of an environmental perturbation such as a change in temperature or surface pressure. To overcome some of the inherent limitations of the generalized 2D method, model-based approaches such as bn-and kn-correlation analyses and the global 2D phase angle method were developed. This review discusses some of the recent applications of these novel methods to Langmuir monolayers of phospholipids and proteins at the air-water interface and Langmuir-Blodgett polymer films.

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Structure and properties of phospholipid–peptide monolayers containing monomeric SP-B1–25

Cited by 33 publications

References 45 publications

Functional importance of the NH₂-terminal insertion sequence of lung surfactant protein B

Functional importance of the NH₂-terminal insertion sequence of lung surfactant protein B

Interactions of KLA Amphipathic Model Peptides with Lipid Monolayers

The application of two‐dimensional correlation spectroscopy to surface and interfacial analysis

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Structure and properties of phospholipid–peptide monolayers containing monomeric SP-B1–25

Cited by 33 publications

References 45 publications

Functional importance of the NH2-terminal insertion sequence of lung surfactant protein B

Functional importance of the NH2-terminal insertion sequence of lung surfactant protein B

Interactions of KLA Amphipathic Model Peptides with Lipid Monolayers

The application of two‐dimensional correlation spectroscopy to surface and interfacial analysis

Contact Info

Product

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Functional importance of the NH₂-terminal insertion sequence of lung surfactant protein B

Functional importance of the NH₂-terminal insertion sequence of lung surfactant protein B