Effects of macromolecular crowding on the structural stability of human α-lactalbumin

Acta Biochimica et Biophysica Sinica

Volumn 44, Issue 8, 2012, Pages 703-711

  Zhang, De Lin ^a   Wu, Ling Jia ^a   Chen, Jie ^a   Liang, Yi ^a  

^a WUHAN UNIVERSITY   (China)

Author keywords

circular dichroism; fluorescence spectroscopy; human lactalbumin; macromolecular crowding; protein stability; trypsin digestion

Indexed keywords

CALCIUM; LACTALBUMIN; MACROGOL DERIVATIVE; PROTEIN; TRYPSIN;

ARTICLE; CALORIMETRY; CHEMISTRY; CIRCULAR DICHROISM; CONFORMATION; HUMAN; MACROMOLECULE; METHODOLOGY; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROFLUOROMETRY; THERMODYNAMICS;

CALCIUM; CALORIMETRY; CIRCULAR DICHROISM; HUMANS; LACTALBUMIN; MACROMOLECULAR SUBSTANCES; MOLECULAR CONFORMATION; POLYETHYLENE GLYCOLS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; TRYPSIN;

EID: 84864479275     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gms052     Document Type: Article

References (52)

1. Zimmerman SB and Minton AP. Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu Rev Biophys Biomol Struct 1993, 22: 27-65. (Pubitemid 23180316)
2. Minton AP. How can biochemical reactions within cells differ from those in test tubes? J Cell Sci 2006, 119: 2863-2869. (Pubitemid 44177864)
3. Zhou HX, Rivas G and Minton AP. Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences. Annu Rev Biophys 2008, 37: 375-397.
4. Minton AP. Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations. J Pharmacol Sci 2005, 94: 1668-1675. (Pubitemid 41360861)
5. Charlton LM, Barnes CO, Li C, Orans J, Young GB and Pielak GJ. Residue-level interrogation of macromolecular crowding effects on protein stability. J Am Chem Soc 2008, 130: 6826-6830. (Pubitemid 351748420)
6. Sasahara K, McPhie P and Minton AP. Effect of dextran on protein stability and conformation attributed to macromolecular crowding. J Mol Biol 2003, 326: 1227-1237. (Pubitemid 36263394)
7. Zhou BR, Liang Y, Du F, Zhou Z and Chen J. Mixed macromolecular crowding accelerates the oxidative refolding of reduced, denatured lyso-zyme: implications for protein folding in intracellular environments. J Biol Chem 2004, 279: 55109-55116. (Pubitemid 40066504)
8. Tokuriki N, Kinjo M, Negi S, Hoshino M, Goto Y, Urabe I and Yomo T. Protein folding by the effects of macromolecular crowding. Protein Sci 2004, 13: 125-133. (Pubitemid 38021147)
9. Spencer DS, Xu K, Logan TM and Zhou HX. Effects of pH, salt, and macromolecular crowding on the stability of FK506-binding protein: an integrated experimental and theoretical study. J Mol Biol 2005, 351: 219-232. (Pubitemid 40973796)
10. Du F, Zhou Z, Mo ZY, Shi JZ, Chen J and Liang Y. Mixed macromolecu-lar crowding accelerates the refolding of rabbit muscle creatine kinase: implications for protein folding in physiological environments. J Mol Biol 2006, 364: 469-482. (Pubitemid 44715934)
11. Stagg L, Zhang SQ, Cheung MS and Stafshede PW. Molecular crowding enhances native structure and stability of a/b protein flavodoxin. Proc Natl Acad Sci USA 2007, 104: 18976-18981.
12. McPhie P, Ni Y and Minton AP. Macromolecular crowding stabilizes the molten globule form of apomyoglobin with respect to both cold and heat unfolding. J Mol Biol 2006, 361: 7-10. (Pubitemid 44041455)
13. Yuan JM, Chyan CL, Zhou HX, Chung TY, Peng H, Ping G and Yang G. The effects of macromolecular crowding on the mechanical stability of protein molecules. Protein Sci 2008, 17: 2156-2166.
14. Christiansen A, Wang Q, Samiotakis A, Cheung MS and Wittung-Stafshede P. Factors defining effects of macromolecular crowding on protein stability: an in vitro/in silico case study using cytochrome c. Biochemistry 2010, 49: 6519-6530.
15. Miklos AC, Li C, Sharaf NG and Pielak GJ. Volume exclusion and soft interaction effects on protein stability under crowded conditions. Biochemistry 2010, 49: 6984-6991.
16. Hong J and Gierasch LM. Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state. J Am Chem Soc 2010, 132: 10445-10452.
17. Aguilar X, Weise CF, Sparrman T, Watz MW and Stafshede PW. Macromolecular crowding extended to a heptameric system: the co-chaperonin protein 10. Biochemistry 2011, 50: 3034-3044.
18. Schlesinger AP, Wang Y, Tadeo X, Millet O and Pielak GJ. Macromolecular crowding fails to fold a globular protein in cells. J Am Chem Soc 2011, 133: 8082-8085.
19. Miklos AC, Sarkar M, Wang Y and Pielak GJ. Protein crowding tunes protein stability. J Am Chem Soc 2011, 133: 7116-7120.
20. Ellis RJ and Minton AP. Protein aggregation in crowded environments. Biol Chem 2006, 387: 485-497. (Pubitemid 44071450)
21. Minton AP. Implications of macromolecular crowding for protein assembly. Curr Opin Struct Biol 2000, 10: 34-39. (Pubitemid 30099324)
22. Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 1989, 6: 87-103. (Pubitemid 19286669)
23. Kuwajima K. The molten globule state of a-lactalbumin. FASEB J 1996, 10: 102-109.
24. Permyakov EA and Berliner LJ. a-Lactalbumin: structure and function. FEBS Lett 2000, 473: 269-274.
25. Ramboarina S and Redfield C. Structural characterisation of the human a-lactalbumin molten globule at high temperature. J Mol Biol 2003, 330: 1177-1188. (Pubitemid 36818912)
26. Kataoka M, Kuwajima K, Tokunaga F and Goto Y. Structural characterization of the molten globule of a-lactalbumin by solution X-ray scattering. Protein Sci 1997, 6: 422-430. (Pubitemid 27079935)
27. Troullier A, Reinstadler D, Dupont Y, Naumann D and Forge V. Transient non-native secondary structures during the refolding of a-lactalbumin detected by infrared spectroscopy. Nat Struct Biol 2000, 7: 78-86. (Pubitemid 30043253)
28. Mok KH, Nagashima T, Day LJ, Hore PJ and Dobson CM. Multiple subsets of side-chain packing in partially folded states of a-lactalbumins. Proc Natl Acad Sci USA 2005, 102: 8899-8904. (Pubitemid 40881050)
29. Yang F, Jr, Zhang M, Chen J and Liang Y. Structural changes of a-lactalbumin induced by low pH and oleic acid. Biochim Biophys Acta 2006, 1764: 1389-1396. (Pubitemid 44279572)
30. Svensson M, Hakansson A, Mossberg AK, Linse S and Svanborg C. Conversion of a-lactalbumin to a protein inducing apoptosis. Proc Natl Acad Sci USA 2000, 97: 4221-4226. (Pubitemid 30226114)
31. Gustafsson L, Leijonhufvud I, Aronsson A, Mossberg A and Svanborg C. Treatment of skin papillomas with topical a-lactalbumin-oleic acid. N Engl J Med 2004, 350: 2663-2672.
32. Zhang M, Yang F, Jr, Yang F, Chen J, Zheng CY and Liang Y. Cytotoxic aggregates of a-lactalbumin induced by unsaturated fatty acid induce apop-tosis in tumor cells. Chem Biol Interact 2009, 180: 131-142.
33. Zhou Z, Yan X, Pan K, Chen J, Xie ZS, Xiao GF and Yang FQ, et al. Fibril formation of the rabbit/human/bovine prion proteins. Biophys J 2011, 101: 1483-1492.
34. Kaplanas RI and Antanavichyus AI. Isolation and purification of a-lactalbumin, a component of lactose synthetase. Biochemistry 1975, 40: 493-495.
35. Nozaka M, Kuwajima K, Nitta K and Sugai S. Detection and characterization of the intermediate on the folding pathway of human a-lactalbumin. Biochemistry 1978, 17: 3753-3758. (Pubitemid 9022585)
36. Permyakov SE, Pershikova IV, Zhadan AP, Goers J, Bakunts AG, Uversky VN and Berliner LJ, et al. Conversion of human a-lactalbumin to an apo-like state in the complexes with basic poly-amino acids: toward understanding of the molecular mechanism of antitumor action of HAMLET. J Proteome Res 2005, 4: 564-569. (Pubitemid 40548164)
37. Stǎ;nciuc N, Râpeanu G, Bahrim G and Aprodu I. pH and heat-induced structural changes of bovine apo-a-lactalbumin. Food Chem 2012, 131: 956 - 963.
38. Liang Y. Applications of isothermal titration calorimetry in protein science. Acta Biochim Biophys Sin 2008, 40: 565-576. (Pubitemid 352009079)
39. Liang Y, Du F, Sanglier S, Zhou BR, Xia Y, Van Dorsselaer A and Maechling C, et al. Unfolding of rabbit muscle creatine kinase induced by acid. A study using electrospray ionization mass spectrometry, isothermal titration calorimetry, and fluorescence spectroscopy. J Biol Chem 2003, 278: 30098-30105. (Pubitemid 36962402)
40. Mo ZY, Zhu YZ, Zhu HL, Fan JB, Chen J and Liang Y. Low micromolar zinc accelerates the fibrillization of human Tau via bridging of Cys-291 and Cys-322. J Biol Chem 2009, 284: 34648-34657.
41. Zhu HL, Fernández C, Fan JB, Shewmaker F, Chen J, Minton AP and Liang Y. Quantitative characterization of heparin binding to Tau protein. Implication for inducer-mediated Tau filament formation. J Biol Chem 2010, 285: 3592-3599.
42. Wu LJ, Xu LR, Liao JM, Chen J and Liang Y. Both the C-terminal poly-lysine region and the farnesylation of K-RasB are important for its specific interaction with calmodulin. PLoS One 2011, 6: e21929.
43. Zhu HL, Meng SR, Fan JB, Chen J and Liang Y. Fibrillization of human Tau is accelerated by exposure to lead via interaction with His-330 and His-362. PLoS One 2011, 6: e25020.
44. Chrysina ED, Brew K and Acharya KR. Crystal structures of apo- and holo-bovine a-lactalbumin at 2.2-A resolution reveal an effect of calcium on inter-lobe interactions. J Biol Chem 2000, 275: 37021-37029. (Pubitemid 32002118)
45. Xie D, Bhakuni V and Freire E. Calorimetric determination of the energetics of the molten globule intermediate in protein folding: apo-a-lactalbumin. Biochemistry 1991, 30: 10673-10678.
46. Minton AP. Excluded volume as a determinant of macromolecular structure and reactivity. Biopolymers 1981, 20: 2093-2120.
47. Rubinstein M and Colby RH. Polymer Physics. England: Oxford University Press, 2003.
48. Zhou Y and Hall CK. Solute excluded-volume effects on the stability of globular proteins: A statistical thermodynamic theory. Biopolymers 1996, 38: 273-284.
49. Knowles DB, LaCroix AS, Deines NF, Shkel I and Record MT, Jr. Separation of preferential interaction and excluded volume effects on DNA duplex and hairpin stability. Proc Natl Acad Sci USA 2011, 108: 12699-12704.
50. Jiao M, Li HT, Chen J, Minton AP and Liang Y. Attractive proteinpolymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria. Biophys J 2010, 99: 914-923.
51. Li C and Pielak GJ. Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditions. J Am Chem Soc 2009, 131: 1368-1369.
52. McGuffee SR and Elcock AH. Diffusion, Crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm. PLoS Comput Biol 2010, 6: e1000694.