Characterization of heparin–protein interaction by saturation transfer difference (STD) NMR
详细信息 查看全文
- 作者：Fei Yu (1)
Sucharita Roy (1)
Enrique Arevalo (1)
John Schaeck (1)
Jason Wang (1)
Kimberly Holte (1)
Jay Duffner (1)
Nur Sibel Gunay (1)
Ishan Capila (1)
Ganesh V. Kaundinya (1) - 关键词：Heparin ; Saturation transfer difference NMR ; Binding epitope ; FGF2 ; FGF10 ; Surface plasmon resonance
- 刊名：Analytical and Bioanalytical Chemistry
- 出版年：2014
- 出版时间：May 2014
- 年：2014
- 卷：406
- 期：13
- 页码：3079-3089
- 全文大小：823 KB
- 参考文献：1. Bitomsky W, Wade RC (1999) Docking of glycosaminoglycans to heparin-binding proteins: validation for aFGF, bFGF, and antithrombin and application to IL-8. J Am Chem Soc 121:3004-013. doi:f">10.1021/ja983319g f="http://dx.doi.org/10.1021/ja983319g" target="_blank" title="It opens in new window">CrossRef
2. Castellot JJ Jr, Hoover RL, Harper PA, Karnovsky MJ (1985) Heparin and glomerular epithelial cell-secreted heparin-like species inhibit mesangial-cell proliferation. Am J Pathol 120:427-35
3. Luster AD (1998) Chemokines—chemotactic cytokines that mediate inflammation. N Engl J Med 338:436-45 f="http://dx.doi.org/10.1056/NEJM199802123380706" target="_blank" title="It opens in new window">CrossRef
4. Perrimon N, Bernfield M (2000) Specificities of heparan sulphate proteoglycans in developmental processes. Nature 404:725-28 f="http://dx.doi.org/10.1038/35008000" target="_blank" title="It opens in new window">CrossRef
5. Parish CR (2006) The role of heparan sulphate in inflammation. Nat Rev Immunol 6:633-43. doi:f">10.1038/nri1918 f="http://dx.doi.org/10.1038/nri1918" target="_blank" title="It opens in new window">CrossRef
6. Waugh DJJ, Wilson C (2008) The interleukin-8 pathway in cancer. Clin Cancer Res 14:6735-741. doi:f">10.1158/1078-0432.ccr-07-4843 f="http://dx.doi.org/10.1158/1078-0432.CCR-07-4843" target="_blank" title="It opens in new window">CrossRef
7. Olson ST, Srinivasan KR, Bjork I, Shore JD (1981) Binding of high affinity heparin to antithrombin III. Stopped flow kinetic studies of the binding interaction. J Biol Chem 256:11073-1079
8. DiGabriele AD, Lax I, Chen DI, Svahn CM, Jaye M, Schlessinger J, Hendrickson WA (1998) Structure of a heparin-linked biologically active dimer of fibroblast growth factor. Nature 393:812-17 f="http://dx.doi.org/10.1038/31741" target="_blank" title="It opens in new window">CrossRef
9. Faham S, Hileman RE, Fromm JR, Linhardt RJ, Rees DC (1996) Heparin structure and interactions with basic fibroblast growth factor. Science 271:1116-120 f="http://dx.doi.org/10.1126/science.271.5252.1116" target="_blank" title="It opens in new window">CrossRef
10. Nelson RM, Cecconi O, Roberts WG, Aruffo A, Linhardt RJ, Bevilacqua MP (1993) Heparin oligosaccharides bind L- and P-selectin and inhibit acute inflammation. Blood 82:3253-258
11. Duensing TD, Van PJPM (1998) Vitronectin binds to the gonococcal adhesin OpaA through a glycosaminoglycan molecular bridge. Biochem J 334:133-39
12. Spillmann D, Witt D, Lindahl U (1998) Defining the interleukin-8-binding domain of heparan sulfate. J Biol Chem 273:15487-5493 f="http://dx.doi.org/10.1074/jbc.273.25.15487" target="_blank" title="It opens in new window">CrossRef
13. Dong J, Peters-Libeu CA, Weisgraber KH, Segelke BW, Rupp B, Capila I, Hernaiz MJ, LeBrun LA, Linhardt RJ (2001) Interaction of the N-terminal domain of apolipoprotein E4 with heparin. Biochemistry 40:2826-834 f="http://dx.doi.org/10.1021/bi002417n" target="_blank" title="It opens in new window">CrossRef
14. Harrop HA, Coombe DR, Rider CC (1994) Heparin specifically inhibits binding of V3 loop antibodies to HIV-1 gp120, an effect potentiated by CD4 binding. AIDS 8:183-92 f="http://dx.doi.org/10.1097/00002030-199402000-00005" target="_blank" title="It opens in new window">CrossRef
15. Rider CC, Coombe DR, Harrop HA, Hounsell EF, Bauer C, Feeney J, Mulloy B, Mahmood N, Hay A, Parish CR (1994) Anti-HIV-1 activity of chemically modified heparins: correlation between binding to the V3 loop of gp120 and inhibition of cellular HIV-1 infection in vitro. Biochemistry 33:6974-980 f="http://dx.doi.org/10.1021/bi00188a029" target="_blank" title="It opens in new window">CrossRef
16. Shukla D, Liu J, Blaiklock P, Shworak NW, Bai X, Esko JD, Cohen GH, Eisenberg RJ, Rosenberg RD, Spear PG (1999) A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell 99:13-2 f="http://dx.doi.org/10.1016/S0092-8674(00)80058-6" target="_blank" title="It opens in new window">CrossRef
17. Janis JS (2012) Glycosaminoglycan and chemokine/growth factor interactions. Handb Exp Pharmacol 207:307-24. doi:f">10.1007/978-3-642-23056-1_13 f="http://dx.doi.org/10.1007/978-3-642-23056-1_13" target="_blank" title="It opens in new window">CrossRef
18. Capila I, Linhardt RJ (2002) Heparin–protein interactions. Angew Chem Int Ed 41:390-12. doi:f">10.1002/1521-3773(20020201)41:3<390::aid-anie390>3.0.co;2-b f="http://dx.doi.org/10.1002/1521-3773(20020201)41:3<390::AID-ANIE390>3.0.CO;2-B" target="_blank" title="It opens in new window">CrossRef
19. Casu B, Lindahl U (2001) Structure and biological interactions of heparin and heparan sulfate. Adv Carbohydr Chem Biochem 57:159-06 f="http://dx.doi.org/10.1016/S0065-2318(01)57017-1" target="_blank" title="It opens in new window">CrossRef
20. Esko JD, Lindahl U (2001) Molecular diversity of heparan sulfate. J Clin Invest 108:169-73. doi:f">10.1172/jci13530 f="http://dx.doi.org/10.1172/JCI200113530" target="_blank" title="It opens in new window">CrossRef
21. Gandhi NS, Mancera RL (2008) The structure of glycosaminoglycans and their interactions with proteins. Chem Biol Drug Des 72:455-82. doi:f">10.1111/j.1747-0285.2008.00741.x f="http://dx.doi.org/10.1111/j.1747-0285.2008.00741.x" target="_blank" title="It opens in new window">CrossRef
22. Lindahl U, Backstrom G, Hook M, Thunberg L, Fransson LA, Linker A (1979) Structure of the antithrombin-binding site in heparin. Proc Natl Acad Sci U S A 76:3198-202 f="http://dx.doi.org/10.1073/pnas.76.7.3198" target="_blank" title="It opens in new window">CrossRef
23. Rosenberg RD, Lam L (1979) Correlation between structure and function of heparin. Proc Natl Acad Sci U S A 76:1218-222. doi:f">10.1073/pnas.76.3.1218 f="http://dx.doi.org/10.1073/pnas.76.3.1218" target="_blank" title="It opens in new window">CrossRef
24. Ashikari-Hada S, Habuchi H, Kariya Y, Itoh N, Reddi AH, Kimata K (2004) Characterization of growth factor-binding structures in heparin/heparan sulfate using an octasaccharide library. J Biol Chem 279:12346-2354. doi:f">10.1074/jbc.M313523200 f="http://dx.doi.org/10.1074/jbc.M313523200" target="_blank" title="It opens in new window">CrossRef
25. Freire E, Mayorga OL, Straume M (1990) Isothermal titration calorimetry. Anal Chem 62:950A-59A. doi:f">10.1021/ac00217a715 f="http://dx.doi.org/10.1021/ac00217a002" target="_blank" title="It opens in new window">CrossRef
26. Ahl I-M, Jonsson B-H, Tibell LAE (2009) Thermodynamic characterization of the interaction between the C-terminal domain of extracellular superoxide dismutase and heparin by isothermal titration calorimetry. Biochemistry 48:9932-940. doi:f">10.1021/bi900981k f="http://dx.doi.org/10.1021/bi900981k" target="_blank" title="It opens in new window">CrossRef
27. Rice KG, Wu P, Brand L, Lee YC (1991) Interterminal distance and flexibility of a triantennary glycopeptide as measured by resonance energy transfer. Biochemistry 30:6646-655. doi:f">10.1021/bi00241a003 f="http://dx.doi.org/10.1021/bi00241a003" target="_blank" title="It opens in new window">CrossRef
28. Capila I, VanderNoot VA, Mealy TR, Seaton BA, Linhardt RJ (1999) Interaction of heparin with annexin V. FEBS Lett 446:327-30. doi:f">10.1016/s0014-5793(99)00245-8 f="http://dx.doi.org/10.1016/S0014-5793(99)00245-8" target="_blank" title="It opens in new window">CrossRef
29. Kumar V, Yadav VK, Hassan MI, Singh AK, Dey S, Singh S, Singh TP, Yadav S (2012) Kinetic and structural studies on the interactions of heparin and proteins of human seminal plasma using surface plasmon resonance. Protein Pept Lett 19:795-03. doi:f">10.2174/092986612801619525 f="http://dx.doi.org/10.2174/092986612801619525" target="_blank" title="It opens in new window">CrossRef
30. Palmer RA, Niwa H (2003) X-ray crystallographic studies of protein–ligand interactions. Biochem Soc Trans 31:973-79. doi:f">10.1042/bst0310973 f="http://dx.doi.org/10.1042/BST0310973" target="_blank" title="It opens in new window">CrossRef
31. Mayer M, Meyer B (2001) Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J Am Chem Soc 123:6108-117. doi:f">10.1021/ja0100120 f="http://dx.doi.org/10.1021/ja0100120" target="_blank" title="It opens in new window">CrossRef
32. Meyer B, Peters T (2003) NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors. Angew Chem Int Ed 42:864-90. doi:f">10.1002/anie.200390233 f="http://dx.doi.org/10.1002/anie.200390233" target="_blank" title="It opens in new window">CrossRef
33. Marco G, Stefano E, Pierre M, Timothy RR, Davide G, Benito C, Christian B, Giangiacomo T, Christian V (2013) An unusual antithrombin-binding heparin octasaccharide with an additional 3-O-sulfated glucosamine in the active pentasaccharide sequence. Biochem J 449(2):343-51. doi:f">10.1042/bj20121309 f="http://dx.doi.org/10.1042/BJ20121309" target="_blank" title="It opens in new window">CrossRef
34. Christian V, Stefano E, Elena U, Davide G, Pierre M, Frederic H, Christian B, Benito C, Giangiacomo T, Marco G (2013) Heparin dodecasaccharide containing two antithrombin-binding pentasaccharides: structural features and biological properties. J Biol Chem 288(36):25895-5907. doi:f">10.1074/jbc.M113.485268 f="http://dx.doi.org/10.1074/jbc.M113.485268" target="_blank" title="It opens in new window">CrossRef
35. Viegas A, Manso J, Nobrega FL, Cabrita EJ (2011) Saturation-transfer difference (STD) NMR: a simple and fast method for ligand screening and characterization of protein binding. J Chem Educ 88:990-94. doi:f">10.1021/ed101169t f="http://dx.doi.org/10.1021/ed101169t" target="_blank" title="It opens in new window">CrossRef
36. Meyer B, Klein J, Mayer M, Meinecke R, M?ller H, Neffe A, Schuster O, Wülfken J, Ding Y, Knaie O, Labbe J, Palcic MM, Hindsgaul O, Wagner B, Ernst B (2004) Saturation transfer difference NMR spectroscopy for identifying ligand epitopes and binding specificities. In: Hamann A, Asadullah K, Schottelius A (eds) Leucocyte trafficking, vol 44. Ernst Schering Research Foundation Workshop, Springer Berlin Heidelberg, pp 149-67. doi:f">10.1007/978-3-662-05397-3_9 f="http://dx.doi.org/10.1007/978-3-662-05397-3_9" target="_blank" title="It opens in new window">CrossRef
37. Jayalakshmi V, Krishna NR (2002) Complete relaxation and conformational exchange matrix (CORCEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand-receptor complexes. J Magn Reson 155(1):106-18. doi:f">10.1006/jmre.2001.2499 f="http://dx.doi.org/10.1006/jmre.2001.2499" target="_blank" title="It opens in new window">CrossRef
38. Thompson LD, Pantoliano MW, Springer BA (1994) Energetic characterization of the basic fibroblast growth factor-heparin interaction: identification of the heparin binding domain. Biochemistry 33:3831-840. doi:f">10.1021/bi00179a006 f="http://dx.doi.org/10.1021/bi00179a006" target="_blank" title="It opens in new window">CrossRef
39. Guglieri S, Hricovíni M, Raman R, Polito L, Torri G, Casu B, Sasisekharan R, Guerrini M (2008) Minimum FGF2 binding structural requirements of heparin and heparan sulfate oligosaccharides as determined by NMR spectroscopy. Biochemistry 47(52):13862-3869. doi:f">10.1021/bi801007p f="http://dx.doi.org/10.1021/bi801007p" target="_blank" title="It opens in new window">CrossRef - 作者单位：Fei Yu (1)
Sucharita Roy (1)
Enrique Arevalo (1)
John Schaeck (1)
Jason Wang (1)
Kimberly Holte (1)
Jay Duffner (1)
Nur Sibel Gunay (1)
Ishan Capila (1)
Ganesh V. Kaundinya (1)
1. Momenta Pharmaceuticals, Inc. 475 West Kendall Street, 02142, Cambridge, MA, USA - ISSN：1618-2650
文摘
The binding affinity and specificity of heparin to proteins is widely recognized to be sulfation-pattern dependent. However, for the majority of heparin-binding proteins (HBPs), it still remains unclear what moieties are involved in the specific binding interaction. Here, we report our study using saturation transfer difference (STD) nuclear magnetic resonance (NMR) to map out the interactions of synthetic heparin oligosaccharides with HBPs, such as basic fibroblast growth factor (FGF2) and fibroblast growth factor 10 (FGF10), to provide insight into the critical epitopes of heparin ligands involved. The irradiation frequency of STD NMR was carefully chosen to excite the methylene protons so that enhanced sensitivity was obtained for the heparin–protein complex. We believe this approach opens up additional application avenues to further investigate heparin–protein interactions.