Molecular dynamics and circular dichroism studies of human and rat C-peptides

Journal of Molecular Graphics and Modelling

Volumn 25, Issue 4, 2006, Pages 532-542

  Mares Guia, Thiago Rennó ^a   Maigret, Bernard ^b,c   Martins, Natália Florêncio ^d   Maia, Ana Luiza Turchetti ^a   Vilela, Luciano ^e   Ramos, Carlos Henrique Inácio ^f   Neto, Luiz Juliano ^g   Juliano, Maria Aparecida ^g   dos Mares Guia, Marcos Luiz ^a,e   Santoro, Marcelo Matos ^a  

^a FEDERAL UNIVERSITY OF MINAS GERAIS   (Brazil)

^b NANCY UNIVERSITÉ   (France)

^c UNIVERSITY OF BRASILIA   (Brazil)

^d EMBRAPA RECURSOS GENÉTICOS E BIOTECNOLOGIA   (Brazil)

^e Biomm SA   (Brazil)

^f LABORATÓRIO NACIONAL DE LUZ SÍNCROTRON   (Brazil)

^g FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

C peptide; Circular dichroism; Diabetes mellitus; Homology building; Molecular dynamics

Indexed keywords

BIODIVERSITY; COMPUTER SIMULATION; CONFORMATIONS; HORMONES; MOLECULAR DYNAMICS; PATIENT TREATMENT; PHYSIOLOGICAL MODELS;

CIRCULAR DICHROISM (CD); DIABETES MELLITUS; HOMOLOGY; TERTIARY STRUCTURES;

POLYPEPTIDES;

C PEPTIDE; TRIFLUOROETHANOL; WATER;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; COMPARATIVE STUDY; CONTROLLED STUDY; HUMAN; HUMAN CELL; MOLECULAR DYNAMICS; MOLECULE; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; RAT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SIMULATION; THEORETICAL MODEL; VACUUM; VALIDATION PROCESS;

AMINO ACID SEQUENCE; ANIMALS; C-PEPTIDE; CIRCULAR DICHROISM; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; RATS; SEQUENCE ALIGNMENT; THERMODYNAMICS;

MAMMALIA;

EID: 33750594279     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2006.03.002     Document Type: Article

References (47)

1. Steiner D.F., Cunningham D., Spigelman L., and Aten B. Insulin biosynthesis: evidence for a precursor. Science 157 (1967) 697-700
2. Oyer P.E., Cho S., Peterson J.D., and Steiner D.F. Studies on human proinsulin: Isolation and aminoacid sequence of the human pancreatic C-peptide. J. Biol. Chem. 246 (1971) 1375-1386
3. Chan S.J., Keim P., and Steiner D.F. Cell-free synthesis of rat preproinsulins: characterization and partial amino acid sequence determination. Proc. Natl. Acad. Sci. U.S.A. 73 (1976) 1964-1968
4. Steiner D.F. On the role of the proinsulin C-peptide. Diabetes 27 (1978) 145-148
5. Davidson H.W., Rhodes C.J., and Hutton J.C. Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic beta cell via two distinct site-specific endopeptidases. Nature 333 (1988) 93-96
6. Rubenstein A.H., Clark J.L., Melani F., and Steiner D.F. Secretion of proinsulin C-peptide by pancreatic beta cells and its circulation in blood. Nature 224 (1969) 697-699
7. Weiss M.A., Frank B.H., Khait I., Pekar A., Heiney R., Shoelson S.E., and Neuringer L.J. NMR and photo-CIDNP studies of human proinsulin and prohormone processing intermediates with application to endopeptidase recognition. Biochemistry 29 (1990) 8389-8401
8. Chen L.M., Yang X.W., and Tang J.G. Acidic residues on the N-terminus of proinsulin C-peptide are important for the folding of insulin precursor. J. Biochem. 131 (2002) 855-859
9. Qiao Z.S., Min C.Y., Hua Q.X., Weiss M.A., and Feng Y.M. In vitro refolding of human proinsulin. J. Biol. Chem. 278 (2003) 17800-17809
10. Kitabchi A.E. Proinsulin and C-peptide: a review. Metabolism 26 (1977) 547-587
11. Ido Y., Vindigni A., Chang K., Stramm L., Chance R., Heath W.F., DiMarchi R.D., Di Cera E., and Williamson J.R. Prevention of vascular and neural dysfunction in diabetic rats by C-peptide. Science 277 (1997) 563-566
12. Wahren J., Ekberg K., Johansson J., Henriksson M., Pramanik A., Johansson B.L., Rigler R., and Jörnvall H. Role of C-peptide in human physiology. Am. J. Physiol. Endocrinol. Metab. 278 (2000) 759-768
13. Wahren J. C-peptide: new findings and therapeutic implications in diabetes. Clin. Physiol. Funct. Imaging 24 (2004) 180-189
14. Rigler R., Pramanik A., Jonasson P., Kratz G., Jansson O.T., Nygren P.-A., Ståhl S., Ekberg K., Johansson B.-L., Uhlén S., Uhlén M., Jörnvall H., and Wahren J. Specific binding of proinsulin C-peptide to human cell membranes. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 13318-31323
15. +-ATPase via activation of ERK1/2 MAP kinases in human renal tubular cells. Cell. Mol. Life Sci. 61 (2004) 2782-2790
16. Zhong Z., Davidescu A., Ehrén I., Ekberg K., Jörnvall H., Wahren J., and Chibalin A.V. C-peptide stimulates ERK1/2 and JNK MAP kinases via activation of protein kinase C in human renal tubular cells. Diabetologia 48 (2005) 187-197
17. Markussen J. Structural changes involved in the folding of proinsulin. Int. J. Protein Res. 3 (1971) 201-207
18. Frank B.H., Pekar A.H., and Veros A.J. Insulin and proinsulin conformation in solution. Diabetes 21 (1972) 486-491
19. Fullerton W.W., Potter R., and Low B.W. Proinsulin: crystallization and preliminary X-ray diffraction studies. Proc. Natl. Acad. Sci. U.S.A. 66 (1970) 1213-1219
20. Snell C.R., Smyth D.G., and Proinsulin:. A proposed three-dimensional structure. J. Biol. Chem. 250 (1975) 6291-6295
21. Lipkind G., and Steiner D.F. Predicted structural alterations in proinsulin during its interactions with prohormone convertases. Biochemistry 38 (1999) 890-896
22. Naithani V.K., Dechesne M., Markussen J., and Heding L.G. Improved synthesis of human proinsulin C-peptide and its benzyloxycarbonyl derivative. Circular dichroism and immunological studies of human C-peptide. Hoppe-Seyler's Z. Physiol. Chem. 356 (1975) 997-1010
23. Xie L., and Tsou C.-L. Comparison of secondary structures of insulin and proinsulin by FT-IR. J. Protein Chem. 12 (1993) 483-487
24. Henriksson M., Shafqat J., Liepinsh E., Tally M., Wahren J., Jörnvall H., and Johansson J. Unordered structure of proinsulin C-peptide in aqueous solution and in the presence of lipid vesicles. Cell. Mol. Life Sci. 57 (2000) 337-342
25. Benson D.A., Karsch-Mizrachi I., Lipman D.J., Ostell J., and Wheeler D.L. GenBank: Update. Nucl. Acids Res. 32 (2004) 23-26
26. Apweiler R., Bairoch A., Wu C.H., Barker W.C., Boeckmann B., Ferro S., Gasteiger E., Huang H., Lopez R., Magrane M., Martin M.J., Natale D.A., O'Donovan C., Redaschi N., and Yen L.S. Uniprot: the universal protein knowledgebase. Nucl. Acids Res. 32 (2004) 115-119
27. Chenna R., Sugawara H., Koike T., Lopez R., Gibson T.J., Higgins D.G., and Thompson J.D. Multiple sequence alignment with the Clustal series of programs. Nucl. Acids Res. 31 (2003) 3497-3500
28. Campanella J.J., Bitincka L., and Smalley J. MatGAT: an application that generates similarity/identity matrices using protein or DNA sequences. BMC Bioinformat. 4 (2003) 29
29. Combet C., Blanchet C., Geourjon C., and Deléage G. NPS@: Network protein sequence analysis. Trends Biochem. Sci. 25 (2000) 147-150
30. Berman H.M., Westbrook J., Feng Z., Gilliland G., Bhat T.N., Weissig H., Shindyalov I.N., and Bourne P.E. The protein data bank. Nucl. Acids Res. 28 (2000) 235-242
31. Pearson W.R., and Lipman D.J. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 2444-2448
32. Insight II, Discover force fields CVFF and CFF91, Accelrys Corp., San Diego, CA, USA.
33. Chen G.C., and Yang J.T. Two-point calibration of circular dichrometer with d-10-camphorsulfonic acid. Anal. Lett. 10 (1977) 1195-1207
34. Reed J., and Reed T.A. A set of constructed type spectra for the practical estimation of peptide secondary structure from circular dichroism. Anal. Biochem. 254 (1997) 36-40
35. Andrade M.A., Chacón P., Merelo J.J., and Morán F. Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network. Prot. Eng. 6 (1993) 383-390
36. Forood B., Feliciano E.J., and Nambiar K.P. Stabilization of α-helical structures in short peptides via end capping. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 838-842
37. Kaufmann J.E., Irminger J.C., and Halban P.A. Sequence requirements for proinsulin processing at the B-chain/C-peptide junction. Biochem. J. 310 (1995) 869-874
38. Jas G.S., and Kuczera K. Equilibrium structure and folding of a helix-forming peptide: circular dichroism measurements and replica-exchange molecular dynamics simulations. Biophys. J. 87 (2004) 3786-3798
39. Raut V.P., Agashe M.A., Stuart S.J., and Latour R.A. Molecular dynamics simulations of peptide-surface interactions. Langmuir 21 (2005) 1629-1639
40. Khandelia H., and Kaznessis Y.N. Molecular dynamics simulations of helical antimicrobial peptides in SDS micelles: what do point mutations achieve?. Peptides 26 (2005) 2037-2049
41. Munte C.E., Vilela L., Kalbitzer H.R., and Garratt R.C. Solution structure of human proinsulin C-peptide. FEBS J. 272 (2005) 4284-4293
42. Markussen J., and Schiff H.E. Molecular parameters of C-peptide from bovine proinsulin. Int. J. Peptide Protein Res. 5 (1973) 69-72
43. Vogt H.-P., Wollmer A., Naithani V.K., and Zahn H. The conformational potential of porcine proinsulin C-peptide. Hoppe-Seyler's Z. Physiol. Chem. 357 (1976) 107-116
44. Blundell T.L., Dodson G.G., Hodgkin D.C., and Mercola D.A. Insulin: the structure in the crystal and its reflection in chemistry and biology. Adv. Prot. Chem. 26 (1972) 279-402
45. Steiner D.F. The proinsulin C-peptide-a multirole model. Exp. Diabesity Res. 5 (2004) 7-14
46. Markussen J., and Volund A. Conformation analysis of circular dichroism spectra of insulin, proinsulin and c-peptides by non-linear regression. Int. J. Peptide Protein Res. 7 (1975) 47-56
47. Woody R.W. Circular dichroism. In: Sauer K. (Ed). Methods in Enzymology vol. 246 (1995), Academic Press, New York 34-71