Molecular Structures and Interactions of Pulmonary Surfactant Components

Johansson, Jan; Curstedt, Tore

doi:10.1111/j.1432-1033.1997.00675.x

Cited by 269 publications

(230 citation statements)

References 197 publications

(212 reference statements)

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“…However, SP-C(Leu), in contrast to native SP-C, undergoes oligomerization tant is estimated to be maximally a few grams/100 g, see [6]. SP-B has been shown to specifically interact with PamOH in both in solution and in the presence of SDS and down to at least low micromolar concentrations (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…All side-chain-protecting groups (except a Trp-protecting formyl group, see below) were removed constitute a hydrophobic protein core which is not exposed to the solvent [8]. This structure does not explain how the hy-and the peptides liberated from the synthesis resin by cleavage with anhydrous hydrogen fluoride/anisol/dimethylsulphide, drophobic and dimeric SP-B interacts with phospholipid bilayers [6,7,9]. SP-C is a 4.2-kDa lipopeptide.…”

mentioning

confidence: 99%

“…The protecting formyl group of the WMAP10 Trp8 imino group A-helix is oriented in a transmembrane way in a fluid phospholipid bilayer [6] where the poly-valyl helical part may interact was removed by incubation of the peptide (5 mg/ml) in 0.4 M ethanolamine/6 M guanidine/HCl, pH 11, at 0°C for 5 min, optimally with the fatty acyl-chains [13]. In a Pam 2 GroPCho monolayer, the SP-C helix makes an approximately 70°tilt rela-whereafter the reaction was stopped by the addition of HCl until the pH reached 6.0.…”

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confidence: 99%

“…The lipids were used without further purification since purity checks by thin-layer chromastructural properties [6]. SP-B is a 17.4-kDa homodimer, composed of two 79-residue polypeptides that each contain three tography showed single spots.…”

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Synthetic peptide‐containing surfactants

Nilsson

Gustafsson

Vandenbussche

et al. 1998

European Journal of Biochemistry

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Pulmonary surfactant contains two hydrophobic proteins, SP-B and SP-C. With the aim of identifying synthetic SP-B and SP-C substitutes for replacement therapy of respiratory distress syndromes, we have studied two transmembrane peptides and two amphipathic peptides that are located in the plane of a phospholipid bilayer. One amphipathic peptide was designed by changing the amino acid sequence, but not the composition or size, of the 21-residue peptide KL 4 . This peptide, designated KL 2.3 from its spacing of nonpolar and polar residues, exhibited similar A-helical content as KL 4 but was oriented along a phospholipid bilayer plane, in contrast to the transmembrane orientation of KL 4 in the same environment. The second amphipathic peptide analyzed was succinyl-LLEKLLEWLK-amide (WMAP10). KL 4 more efficiently accelerated the spreading of a mixture of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (Pam 2 -GroPCho)/phosphatidylglycerol (PtdGro)/palmitic acid (PamOH), 68:22:9 (by mass), at an air/water interface than did any of the amphipathic peptides. Similarly, KL 4 , but not KL 2.3 , when present in an interfacial monolayer composed of Pam 2GroPCho/1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol, 7: 3 (by mass), increased lipid insertion from subphase vesicles.An SP-C analogue, SP-C(Leu), with all helical valyl residues in native SP-C replaced with Leu and the palmitoylcysteines at positions 5 and 6 replaced with Ser, but otherwise with essentially the same primary structure as the native peptide, was analyzed. SP-C(Leu) exhibited similar A-helical content as native SP-C and a transmembrane orientation and, in contrast to poly-valyl-containing synthetic peptides, it folds into a helical conformation after acid-induced denaturation. SP-C(Leu) accelerated the spreading of Pam 2 GroPCho/PtdGro/PamOH, 68:22:9 (by mass), almost identically to native SP-C, and lowered the surface tension during rapid cyclic film compressions in a pulsating bubble surfactometer to near zero and 43 mN/m at minimum and maximum bubble size, respectively. Airway instillation of 2% (by mass) SP-C(Leu) combined with Pam 2 GroPCho/PtdGro/PamOH in preterm rabbit fetuses improved dynamic lung compliance by about 30% compared with untreated controls.Keywords : pulmonary surfactant; surfactant protein B ; surfactant protein C ; transmembrane peptide; amphipathic peptide.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

mentioning

confidence: 99%

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Synthetic peptide‐containing surfactants

Nilsson

Gustafsson

Vandenbussche

et al. 1998

European Journal of Biochemistry

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“…Pulmonary surfactant collected by lavage consists mainly of lipids such as dipalmitoylphosphatidylcholine (DPPC), phosphatidylglycerol (PG), and small amounts of the surfactant-associated proteins (SP-) SP-A, SP-B, SP-C, and SP-D (see Johansson and Curstedt, 1997;Possmayer, 1997;for recent reviews). TM can be reconstituted in vitro using DPPC and PG and the surfactant apoproteins SP-A and SP-B, under the influence of millimolar concentrations of calcium (Efrati et al, 1987;Suzuki et al, 1989;Williams et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Correlated Atomic Force and Transmission Electron Microscopy of Nanotubular Structures in Pulmonary Surfactant

Nag

Munro

Hearn

et al. 1999

Journal of Structural Biology

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Pulmonary surfactant stabilizes the lung by reducing surface tension at the air-water interface of the alveoli. Surfactant is present in the lung in a number of morphological forms, including tubular myelin (TM). TM is composed of unusual 40 ؋ 40 nm square elongated proteolipid tubes. Atomic force microscopy (AFM) was performed on polymerembedded Lowicryl and London Resin-White (LRWhite) unstained thin sections. AFM was used in imaging regions of the sections where TM was detected by transmission electron microscopy (EM) of corresponding stained sections. Tapping-and contact-mode AFM imaging of the unstained sections containing TM indicated a highly heterogeneous surface topography with height variations ranging from 10 to 100 nm. In tapping-mode AFM, tubular myelin was seen as hemispherical protrusions of 30-70 nm in diameter, with vertical dimensions of 5-8 nm. In contact-mode AFM and with phase imaging using a sharper (G10 nm nominal radius) probe, square open-ended tubes which resembled typical electron micrographs of such regions were observed. The cross-hatch structures observed inside the tubes using EM were not observed using AFM, although certain multilobe structures and topographic heterogeneity were detected inside some tubes. Other regions of multilamellar bodies and some regions where such bilayer lamella appear to fuse with the tubes were found in association with TM using AFM. EM of acetone-delipidated tubes in LR-White revealed rectangular tubular cores containing cross-hatched structures, presumably protein skeletons. AFM surface topography of these regions showed hollow depressions at positions at which the protein was anticipated instead of the protrusions seen in the lipid-containing sections. Gold-labeled antibody to surfactant protein A was found associated somewhat randomly within the regions containing the protein skeletons. The topography of the gold particles was observed as sharp peaks in contact-mode AFM. This study suggests a method for unambiguous detection of threedimensional nanotubes present in low abundance in a biological macromolecular complex. Only limited detection of proteins and lipids in surfaces of embedded tubular myelin was possible. EM and AFM imaging of such unusual biological structures may suggest unique lipid-protein associations and arrangements in three dimensions. Academic Press

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Characterisation of variant forms of prophenin: mechanistic aspects of the fragmentation of proline-rich peptides

Johansson

Griffiths

2000

Rapid Commun. Mass Spectrom.

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Prophenin 1 (PF‐1) is a 79‐residue polypeptide originally isolated from porcine leukocytes. Its amino acid sequence has been determined by a combination of mass spectrometry and Edman degradation (Harwig SSL. et al. FEBS Lett. 1995; 362: 65). Prophenin (PF) and variants thereof are also found in organic extracts of porcine pulmonary tissue (Wang Y. et al. FEBS Lett. 1999; 460: 257). In the present study we have characterised the variant forms of PF found in these extracts using nano‐electrospray (nano‐ES) high resolution and tandem mass spectrometry. The major forms of PF found in these extracts by nano‐ES mass spectrometry are the 80‐residue polypeptides prophenin‐2‐Pyr (PF‐2‐Pyr) and prophenin‐2‐Gln (PF‐2‐Gln). Prophenin‐2‐Pyr is refractory to Edman degradation due to the presence of an N‐terminal pyroglutamic residue. In PF‐2‐Gln the N‐terminal residue is glutamine and the C‐terminus is amidated. In porcine pulmonary extracts PF‐1 is present to only a minor extent. Other shorter polypeptides are also found in these extracts including 18‐ and 17‐residue C‐terminal fragments of PF. The primary structure of PF is highly unusual in that it shows four almost perfect decamer repeats of FPPPN(V/F)PGPR and, out of the 79/80 residues, 42 are proline and 14 are phenylalanine. Tryptic digestion of PF gives peptides containing the decamer repeat and collision‐induced dissociation of these peptides provides an insight into the fragmentation mechanisms of proline‐rich peptides. Facile cleavage within the Pro‐Pro‐Pro sequence of these peptides suggests the involvement of a cyclic peptide in the fragmentation mechanism. Fragmentation mechanisms that account for the formation of fragment ions at other cleavage sites are also discussed. Copyright © 2000 John Wiley & Sons, Ltd.

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Molecular Structures and Interactions of Pulmonary Surfactant Components

Cited by 269 publications

References 197 publications

Synthetic peptide‐containing surfactants

Synthetic peptide‐containing surfactants

Correlated Atomic Force and Transmission Electron Microscopy of Nanotubular Structures in Pulmonary Surfactant

Characterisation of variant forms of prophenin: mechanistic aspects of the fragmentation of proline-rich peptides

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