Evaluation of lipid-binding properties of the N-terminal helical segments in human apolipoprotein A-I using fragment peptides

Journal of Peptide Science

Volumn 15, Issue 1, 2009, Pages 36-42

  Tanaka, Masafumi ^a   Tanaka, Toshitaka ^a   Ohta, Shinya ^a   Kawakami, Toru ^b   Konno, Hiroyuki ^c   Akaji, Kenichi ^c   Aimoto, Saburo ^b   Saito, Hiroyuki ^a  

^a KOBE PHARMACEUTICAL UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c KYOTO PREFECTURAL UNIVERSITY OF MEDICINE   (Japan)

Author keywords

ApoA I; Peptide lipid interaction; Proline substitution; Synthetic peptide

Indexed keywords

APOLIPOPROTEIN A1; LIPID; TRIFLUOROETHANOL; TYROSINE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING KINETICS; CIRCULAR DICHROISM; CONTROLLED STUDY; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE; SPECTROSCOPY; THERMODYNAMICS;

AMINO ACID SEQUENCE; APOLIPOPROTEIN A-I; CALORIMETRY; CIRCULAR DICHROISM; HUMANS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS; TITRIMETRY;

EID: 61749099904     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1092     Document Type: Article

References (41)

1. Lewis GF, Rader DJ. New insights into the regulation of HDL metabolism and reverse cholesterol transport. Circ. Res. 2005; 96: 1221-1232
2. Lewis GF. Determinants of plasma HDL concentrations and reverse cholesterol transport. Curr. Opin. Cardiol. 2006; 21: 345-352.
3. Navab M, Anantharamaiah GM, Reddy ST, Van Lenten BJ, Datta G, Garber D, Fogelman AM. Human apolipoprotein A-I and A-I mimetic peptides: potential for atherosclerosis reversal. Curr. Opin. Lipidol. 2004; 15: 645-649.
4. Navab M, Anantharamaiah GM, Reddy ST, Fogelman AM. Apolipoprotein A-I mimetic peptides and their role in atherosclerosis prevention. Nat. Clin. Pract. Cardiovasc. Med. 2006; 3: 540-547.
5. Segrest JP, Jones MK, De Loof H, Brouillette CG, Venkatachalapathi YV, Anantharamaiah GM. The amphipathic helix in the exchangeable apolipoproteins: a review of secondary structure and function. J. Lipid Res. 1992; 33: 141-166.
6. Palgunachari MN, Mishra VK, Lund-Katz S, Phillips MC, Adeyeye SO, Alluri S, Anantharamaiah GM, Segrest JP. Only the two end helixes of eight tandem amphipathic helical domains of human apo A-I have significant lipid affinity. Implications for HDL assembly. Arterioscler. Thromb. Vasc. Biol. 1996; 16: 328-338.
7. Mishra VK, Palgunachari MN, Datta G, Phillips MC, Lund-Katz S, Adeyeye SO, Segrest JP, Anantharamaiah GM. Studies of synthetic peptides of human apolipoprotein A-I containing tandem amphipathic alpha-helixes. Biochemistry 1998; 37: 10313-10324.
8. Natarajan P, Forte TM, Chu B, Phillips MC, Oram JF, Bielicki JK. Identification of an apolipoprotein A-I structural element that mediates cellular cholesterol efflux and stabilizes ATP binding cassette transporter A1. J. Biol. Chem. 2004; 279: 24044-24052.
9. Frank PG, Marcel YL. Apolipoprotein A-I: structure-function relationships. J. Lipid Res. 2000; 41: 853-872.
10. Saito H, Lund-Katz S, Phillips MC. Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins. Prog. Lipid Res. 2004; 43: 350-380.
11. Davidson WS, Hazlett T, Mantulin WW, Jonas A. The role of apolipoprotein AI domains in lipid binding. Proc. Natl. Acad. Sci. U.S.A. 1996; 93: 13605-13610.
12. Saito H, Dhanasekaran P, Nguyen D, Holvoet P, Lund-Katz S, Phillips MC. Domain structure and lipid interaction in human apolipoproteins A-I and E, a general model. J. Biol. Chem. 2003; 278: 23227-23232.
13. Ajees AA, Anantharamaiah GM, Mishra VK, Hussain MM, Murthy HM. Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases. Proc. Natl. Acad. Sci. U.S.A. 2006; 103: 2126-2131.
14. Chou PY, Fasman GD. Prediction of protein conformation. Biochemistry 1974; 13: 222-245.
15. Tanaka M, Dhanasekaran P, Nguyen D, Ohta S, Lund-Katz S, Phillips MC, Saito H. Contributions of the N- and C-terminal helical segments to the lipid-free structure and lipid interaction of apolipoprotein A-I. Biochemistry 2006; 45: 10351-10358.
16. Saito H, Dhanasekaran P, Nguyen D, Deridder E, Holvoet P, Lund-Katz S, Phillips MC. α-Helix formation is required for high affinity binding of human apolipoprotein A-I to lipids. J. Biol. Chem. 2004; 279: 20974-20981.
17. 2, and phosphatidylcholine bilayers. Biochemistry 2002; 41: 4165-4172.
18. Ladokhin AS, Jayasinghe S, White SH. How to measure and analyze tryptophan fluorescence in membranes properly, and why bother? Anal. Biochem. 2000; 285: 235-245.
19. Segall ML, Dhanasekaran P, Baldwin F, Anantharamaiah GM, Weisgraber KH, Phillips MC, Lund-Katz S. Influence of apoE domain structure and polymorphism on the kinetics of phospholipid vesicle solubilization. J. Lipid Res. 2002; 43: 1688-1700.
20. Tanaka M, Koyama M, Dhanasekaran P, Nguyen D, Nickel M, Lund-Katz S, Saito H, Phillips MC. Influence of tertiary structure domain properties on the functionality of apolipoprotein A-I. Biochemistry 2008; 47: 2172-2180.
21. Tanaka M, Saito H, Dhanasekaran P, Wehrli S, Handa T, Lund-Katz S, Phillips MC. Effects of the core lipid on the energetics of binding of apoA-I to model lipoprotein particles of different sizes. Biochemistry 2005; 44: 10689-10695.
22. Zhu HL, Atkinson D. Conformation and lipid binding of a C-terminal (198-243) peptide of human apolipoprotein A-I. Biochemistry 2007; 46: 1624-1634.
23. Li SC, Goto NK, Williams KA, Deber CM. Alpha-helical, but not beta-sheet, propensity of proline is determined by peptide environment. Proc. Natl. Acad. Sci. U.S.A. 1996; 93: 6676-6681.
24. Ponsin G, Hester L, Gotto AM Jr, Pownall HJ, Sparrow JT. Lipid-peptide association and activation of lecithin: cholesterol acyltransferase. Effect of alpha-helicity. J. Biol. Chem. 1986; 261: 9202-9205.
25. Clayton AH, Sawyer WH. The structure and orientation of class-A amphipathic peptides on a phospholipid bilayer surface. Eur. Biophys. J. 1999; 28: 133-141.
26. Lakowicz J. Principles of Fluorescent Spectroscopy. Kluwer Academic/Plenum Publishers: New York, 1999.
27. Gillotte KL, Zaiou M, Lund-Katz S, Anantharamaiah GM, Holvoet P, Dhoest A, Palgunachari MN, Segrest JP, Weisgraber KH, Rothblat GH, Phillips MC. Apolipoprotein-mediated plasma membrane microsolubilization. Role of lipid affinity and membrane penetration in the efflux of cellular cholesterol and phospholipid. J. Biol. Chem. 1999; 274: 2021-2028.
28. Massey JB, Pownall HJ. Role of oxysterol structure on the microdomain-induced microsolubilization of phospholipid membranes by apolipoprotein A-I. Biochemistry 2005; 44: 14376-14384.
29. Fukuda M, Nakano M, Sriwongsitanont S, Ueno M, Kuroda Y, Handa T. Spontaneous reconstitution of discoidal HDL from sphingomyelin-containing model membranes by apolipoprotein A-I. J. Lipid Res. 2007; 48: 882-889.
30. Zhu HL, Atkinson D. Conformation and lipid binding of the N-terminal (1-44) domain of human apolipoprotein A-I. Biochemistry 2004; 43: 13156-13164.
31. Jiang ZG, Gantz D, Bullitt E, McKnight CJ. Defining lipid-interacting domains in the N-terminal region of apolipoprotein B. Biochemistry 2006; 45: 11799-11808.
32. Gazzara JA, Phillips MC, Lund-Katz S, Palgunachari MN, Segrest JP, Anantharamaiah GM, Snow JW. Interaction of class A amphipathic helical peptides with phospholipid unilamellar vesicles. J. Lipid Res. 1997; 38: 2134-2146.
33. Seelig J. Thermodynamics of lipid-peptide interactions. Biochim. Biophys. Acta 2004; 1666: 40-50.
34. Wieprecht T, Apostolov O, Beyermann M, Seelig J. Thermodynamics of the alpha-helix-coil transition of amphipathic peptides in a membrane environment: implications for the peptide-membrane binding equilibrium. J. Mol. Biol. 1999; 294: 785-794.
35. Yang ST, Lee JY, Kim HJ, Eu YJ, Shin SY, Hahm KS, Kim JI. Contribution of a central proline in model amphipathic alpha-helical peptides to self-association, interaction with phospholipids, and antimicrobial mode of action. FEBS J. 2006; 273: 4040-4054.
36. Lagerstedt JO, Budamagunta MS, Oda MN, Voss JC. Electron paramagnetic resonance spectroscopy of site-directed spin labels reveals the structural heterogeneity in the N-terminal domain of apoA-I in solution. J. Biol. Chem. 2007; 282: 9143-9149.
37. Sorci-Thomas MG, Thomas MJ. The effects of altered apolipoprotein A-I structure on plasma HDL concentration. Trends Cardiovasc. Med. 2002; 12: 121-128.
38. Han H, Sasaki J, Matsunaga A, Hakamata H, Huang W, Ageta M, Taguchi T, Koga T, Kugi M, Horiuchi S, Arakawa K. A novel mutant, ApoA-I nichinan (Glu235 → 0), is associated with low HDL cholesterol levels and decreased cholesterol efflux from cells. Arterioscler. Thromb. Vasc. Biol. 1999; 19: 1447-1455.
39. Rogers DP, Roberts LM, Lebowitz J, Datta G, Anantharamaiah GM, Engler JA, Brouillette CG. The lipid-free structure of apolipoprotein A-I: effects of amino-terminal deletions. Biochemistry 1998; 37: 11714-11725.
40. Fang Y, Gursky O, Atkinson D. Structural studies of N- and C-terminally truncated human apolipoprotein A-I. Biochemistry 2003; 42: 6881-6890.
41. Tricerri MA, Behling Agree AK, Sanchez SA, Jonas A. Characterization of apolipoprotein A-I structure using a cysteine-specific fluorescence probe. Biochemistry 2000; 39: 14682-14691.