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S Koppenol

Publications and source records attributed to S Koppenol.

4 recordsLinked to original sources
PubMed1999

Two-dimensional crystallization of streptavidin: in pursuit of the molecular origins of structure, morphology, and thermodynamics.

The streptavidin two-dimensional (2D) crystallization model has served as a paradigm for molecular self-assembly at interfaces. We have developed quantitative Brewster angle microscopy for the in situ measurement of spatially resolved relative protein surface densities. This allows investigation of both the thermodynamics and morphologies of 2D crystal growth. For crystal structure analysis, we employ TEM on grown crystals transferred to solid substrates. Comparison of results between commercially available streptavidin, recombinant streptavidin, and site-directed streptavidin mutants has provided insight into the protein protein and protein-lipid interactions that underlie 2D crystallization.

Crystallization↗
PubMed1998

The interaction of lung annexin I with phospholipid monolayers at the air/water interface.

Lung annexin I (LAI), a calcium-ion-dependent phospholipid-binding protein, has been shown earlier to cause aggregation and fusion of bilayered vesicles containing phospholipids found in lung surfactant, and to be a very likely factor in the assembly of lung surfactant into the lamellar bodies stored in the Type II cell. In this study, we have measured the accumulation of LAI into spread monolayers of some major lipid components of lung surfactant, dipalmitoyl-phosphatidylcholine (DPPC), dipalmitoyl-phosphatidylglycerol (DPPG), palmitoyl-oleyoyl-phosphatidylglycerol (POPG), and selected mixtures, as a function of calcium-ion concentration and surface concentration (degree of packing) of the phospholipid monolayer. The ability of LAI to significantly penetrate such monolayers was calcium-ion-dependent and only occurred in the presence of DPPG or POPG. The relative extent of penetration into DPPG and POPG was directly related to the available free area in the monolayer, penetration being greater with POPG. Fluorescence microscopy measurements revealed that DPPC mixed with either DPPG or POPG caused a change in surface phase behavior in a manner believed to be related to certain types of bilayer fusion. A chemical breakdown product of LAI, LAI-bp, previously found not to cause aggregation and fusion of bilayers, did not exhibit comparable monolayer penetration or surface phase separation to LAI.

Air↗
PubMed1998

Effects of a cationic and hydrophobic peptide, KL4, on model lung surfactant lipid monolayers.

We report on the surface behavior of a hydrophobic, cationic peptide, [lysine-(leucine)4]4-lysine (KL4), spread at the air/water interface at 25 degrees C and pH 7.2, and its effect at very low molar ratios on the surface properties of the zwitterionic phospholipid 1,2-dipalmitoylphosphatidylcholine (DPPC), and the anionic forms of 1-palmitoyl-2-oleoylphosphatidylglycerol (POPG) and palmitic acid (PA), in various combinations. Surface properties were evaluated by measuring equilibrium spreading pressures (pi(e)) and surface pressure-area isotherms (pi-A) with the Wilhelmy plate technique. Surface phase separation was observed with fluorescence microscopy. KL4 itself forms a single-phase monolayer, stable up to a surface pressure pi of 30 mN/m, and forms an immiscible monolayer mixture with DPPC. No strong interaction was detected between POPG and KL4 in the low pi region, whereas a stable monolayer of the PA/KL4 binary mixture forms, which is attributed to ionic interactions between oppositely charged PA and KL4. KL4 has significant effects on the DPPC/POPG mixture, in that it promotes surface phase separation while also increasing pi(e) and pi(max), and these effects are greatly enhanced in the presence of PA. In the model we have proposed, KL4 facilitates the separation of DPPC-rich and POPG/PA-rich phases to achieve surface refinement. It is these two phases that can fulfill the important lung surfactant functions of high surface pressure stability and efficient spreading.

1,2-Dipalmitoylphosphatidylcholine↗