Location of structural transitions in an isotopically labeled lung surfactant SP-B peptide by IRRAS

Biophysical Journal

Volumn 85, Issue 1, 2003, Pages 340-349

  Flach, Carol R ^a,c   Cai, Peng ^a   Dieudonné, Darline ^a   Brauner, Joseph W ^a   Keough, Kevin M W ^b   Stewart, June ^b   Mendelsohn, Richard ^a  

^a Rutgers The State University of New Jersey   (United States)

^b MEMORIAL UNIVERSITY OF NEWFOUNDLAND   (Canada)

^c RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CARBON 13; LUNG SURFACTANT; MYELIN; OXYGEN; SURFACTANT PROTEIN B; WATER;

ABSORPTION SPECTROSCOPY; AIR; ARTICLE; BREATHING; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DIPOLE; HYDROPHOBICITY; INFRARED SPECTROSCOPY; NONHUMAN; PRESSURE; PROTEIN FUNCTION; PROTEIN LIPID INTERACTION; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION; SYNTHESIS;

MAMMALIA; SUIDAE;

EID: 0038311726     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74478-6     Document Type: Article

References (41)

1. Andersson, M., T. Curstedt, H. Jornvall, and J. Johansson. 1995. An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B. FEBS Lett. 362:328-332.
2. Bartlett, G. R. 1959. Phosphorous assay in column chromatography. J. Biol. Chem. 234:466-468.
3. Bi, X., C. R. Flach, J. Perez-Gil, I. Plasencia, D. Andreu, E. Oliveira, and R. Mendelsohn. 2002. Secondary structure and lipid interactions of the N-terminal segment of pulmonary surfactant SP-C in Langmuir films: IR reflection-absorption spectroscopy and surface pressure studies. Biochemistry. 41:8385-8395.
4. 13C isotope labeling of hydrophobic peptides. Origin of the anomalous intensity distribution in the infrared Amide I spectral region of β-sheet structures. J. Am. Chem. Soc. 122:677-683.
5. Bruni, R., H. W. Taeusch, and A. J. Waring. 1991. Surfactant protein B: lipid interactions of synthetic peptides representing the amino-terminal amphipathic domain. Proc. Natl. Acad. Sci. USA. 88:1-6.
6. Clark, J. C., S. E. Wert, C. J. Bachurski, M. T. Stahlman, B. R. Stripp, T. E. Weaver, and J. A. Whitsett. 1995. Targeted disruption of the surfactant protein B gene disrupts surfactant homeostasis, causing respiratory failure in newborn mice. Proc. Natl. Acad. Sci. USA. 92:7794-7798.
7. Cochrane, C. G., and S. D. Revak. 1991. Pulmonary surfactant protein B (SP-B): structure-function relationships. Science. 254:566-568.
8. Curstedt, T., J. Johansson, J. Barros-Soderling, B. Robertson, G. Nilsson, M. Westberg, and H. Jornvall. 1988. Low-molecular-mass surfactant protein type 1. The primary structure of a hydrophobic 8-kDa polypeptide with eight half-cysteine residues. Eur. J. Biochem. 172:521-525.
9. x (x = 6, 8, 10, 2) in monolayer, bulk, and lipid-containing phases. Infrared and circular dichroism studies. J. Am. Chem. Soc. 120:792-799.
10. Dieudonné, D., R. Mendelsohn, R. S. Farid, and C. R. Flach. 2001. Secondary structure in lung surfactant SP-B peptides: IR and CD studies of bulk and monolayer phases. Biochim. Biophys. Acta. 1511:99-112.
11. Ding, J., D. Y. Takamoto, A. von Nahmen, M. M. Lipp, K. Y. C. Lee, A. J. Waring, and J. A. Zasadzinski. 2001. Effects of lung surfactant proteins, SP-B and SP-C, and palmitic acid on monolayer stability. Biophys. J. 80:2262-2272.
12. Dluhy, R. A. 1986. Quantitative external reflection infrared spectroscopic analysis of insoluble monolayers spread at the air-water interface. J. Phys. Chem. 90:1373-1379.
13. Dluhy, R. A., and D. G. Cornell. 1985. In situ measurement of the infrared spectra of insoluble monolayers at the air-water interface. J. Phys. Chem. 89:3195-3197.
14. Flach, C. R., Z. Xu, X. Bi, J. W. Brauner, and R. Mendelsohn. 2001. Improved IRRAS apparatus for studies of aqueous monolayer films: determination of the orientation of each chain in a fatty-acid homologous ceramide-2. Appl. Spectrosc. 55:1060-1066.
15. Goerke, J. 1998. Pulmonary surfactant: functions and molecular composition. Biochim. Biophys. Acta. 1408:79-89.
16. Haagsman, H. P., S. Hawgood, T. Sargeant, D. Buckley, W. R. Tyler, K. Drickamer, and B. J. Benson. 1987. The major lung surfactant protein, SP 28-36, is a calcium-dependent, carbohydrate-binding protein. J. Biol. Chem. 262:13877-13880.
17. Hawgood, S., M. Derrick, and F. Poulain. 1998. Structure and properties of surfactant protein B. Biochim. Biophys. Acta. 1408:150-160.
18. Johansson, J., and T. Curstedt. 1997. Molecular structures and interactions of pulmonary surfactant components. Eur. J. Biochem. 244:675-693.
19. Johansson, J., T. Curstedt, and B. Robertson. 2001. Artificial surfactants based on analogues of SP-B and SP-C. Pediatr. Pathol. Mol. Med. 20:501-518.
20. Keough, K. M., and N. Kariel. 1987. Differential scanning calorimetric studies of aqueous dispersions of phophatidylcholines containing two polyenoic chains. Biochim. Biophys. Acta. 902:11-18.
21. Keough, K., S. Taneva, F. J. Walther, and A. Waring. 2002. Adsorption of lung surfactant protein SP-A to lipid monolayers containing N-terminal segments of surfactant protein SP-B causes segregation of a protein-rich surface phase. Biophys. J. 82:8a.
22. 13C isotopically labeled peptide β-sheets comes from extended, multiple-stranded structures. An ab initio study. J. Am. Chem. Soc. 123:6142-6150.
23. Liepinsh, E., M. Andersson, J. M. Ruysschaert, and G. Otting. 1997. Saponsin fold revealed by the NMR structure of NK-lysin. Nat. Struct. Biol. 4:793-795.
24. Longo, M. L., A. M. Bisagno, J. A. N. Zasadzinski, R. Bruni, and A. J. Waring. 1993. A function of lung surfactant protein SP-B. Science. 261:453-456.
25. Mendelsohn, R., and C. R. Flach. Infrared reflection-absorption spectroscopy of lipid, peptides, and proteins in aqueous monolayers. In Current Topics in Membranes, Vol. 52. S. A. Simon and T. J. McIntosh, editors. Academic Press, San Diego. pp. 57-88.
26. Nogee, L. M., G. Garnier, H. C. Dietz, L. Singer, A. M. Murphy, D. E. deMello, and H. R. Colten. 1994. A mutation in the surfactant protein B gene responsible for fatal neonatal respiratory disease in multiple kindreds. J. Clin. Invest. 93:1860-1863
27. Pastrana-Rios, B., S. Taneva, K. M. W. Keough, A. J. Mautone, and R. Mendelsohn. 1995. External reflection absorption infrared spectroscopy study of lung surfactant proteins SP-B and SP-C in phospholipid monolayers at the air/water interface. Biophys. J. 69:2531-2540.
28. Patthy, L. 1991. Homology of the precursor of pulmonary surfactant-associated protein SP-B with prosaposin and sulfated glycoprotein-1. J. Biol. Chem. 266:6035-6037.
29. Pérez-Gil, J., and K. M. W. Keough. 1998. Interfacial properties of surfactant proteins. Biochim. Biophys. Acta. 1408:203-217.
30. Robertson, B., and H. L. Halliday. 1998. Principles of surfactant therapy. Biochim. Biophys. Acta. 1408:346-361.
31. Rost, B., and C. Sander. 1993a. Improved prediction of protein secondary structure by use of sequence profiles and neural networks. Proc. Natl. Acad. Sci. USA. 90:7558-7562.
32. Rost, B., and C. Sander. 1993b. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232:584-599.
33. Rost, B., and C. Sander. 1994. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins. 19:55-72.
34. Sarin, V. K., S. Gupta, T. K. Leung, V. E. Taylor, B. L. Ohning, J. A. Whitsett, and J. L. Fox. 1990. Biophysical and biological activity of a synthetic 8.7-kDa hydrophobic pulmonary surfactant protein SP-B. Proc. Natl. Acad. Sci. USA. 87:2633-2637.
35. Taneva, S., and K. M. W. Keough. 1994. Pulmonary surfactant proteins SP-B and SP-C in spread monolayers at the air-water interface. 1. Monolayers of pulmonary surfactant protein SP-B and phospholipids. Biophys. J. 66:1137-1148.
36. Taneva, S., T. McEachren, J. Stewart, and K. M. W. Keough. 1995. Pulmonary surfactant protein SP-A with phospholipids in spread monolayers at the air-water interface. Biochemistry. 34:10279-10289.
37. Tokieda, K., J. A. Whitsett, J. C. Clark, T. E. Weaver, K. Ikeda, K. B. McConnell, A. H. Jobe, M. Ikegami, and H. S. Iwamoto. 1997. Pulmonary dysfunction in neonatal SP-B-deficient mice. Am. J. Physiol. 273:L875-L882.
38. Udenfriend, S., S. Stein, P. Bohlen, W. Dairman, W. Leimgruber, and M. Weigele. 1972. Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range. Science. 178:871-872.
39. Veldhuizen, E. J. A., A. J. Waring, F. J. Walther, J. J. Batenburg, L. M. G. van Golde, and H. P. Haagsman. 2000. Dimeric N-terminal segment of human surfactant protein B (dSP-B 1-25) has enhanced surface properties compared to monomeric SP-B 1-25. Biophys. J. 79:377-384.
40. Weaver, T. E., and J. J. Conkright. 2001. Functions of surfactant proteins B and C. Annu. Rev. Physiol. 63:555-578.
41. Wilson, E. B., Jr., J. C. Decius, and P. C. Cross. 1955. Molecular Vibrations. McGraw-Hill, New York.