Pinpointing proline substitution to be responsible for the loss of amyloidogenesis in IAPP

Chemical Biology and Drug Design

Volumn 82, Issue 4, 2013, Pages 446-452

  Chakraborty, Sandipan ^a   Mukherjee, Barnali ^b   Basu, Soumalee ^c,d  

^a Saroj Mohan Institute of Technology   (India)

^b JADAVPUR UNIVERSITY   (India)

^c MAULANA ABUL KALAM AZAD UNIVERSITY OF TECHNOLOGY   (India)

^d UNIVERSITY OF CALCUTTA   (India)

Author keywords

Aggregation; Fibril; Human type II diabetes; IAPP; Molecular dynamics; Proline substitution

Indexed keywords

AMYLIN; AMYLOID; PROLINE; VALINE;

AMINO ACID SUBSTITUTION; AMYLOIDOGENESIS; ARTICLE; BIOGENESIS; HUMAN; MOLECULAR DYNAMICS; MOLECULAR EVOLUTION; MUTATION; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; WILD TYPE;

RODENTIA;

AGGREGATION; FIBRIL; HUMAN TYPE II DIABETES; IAPP; MOLECULAR DYNAMICS; PROLINE SUBSTITUTION;

AMYLOID; HUMANS; ISLET AMYLOID POLYPEPTIDE; MOLECULAR DYNAMICS SIMULATION; PROLINE; PROTEIN STRUCTURE, SECONDARY;

EID: 84884817264     PISSN: 17470277     EISSN: 17470285     Source Type: Journal    
DOI: 10.1111/cbdd.12172     Document Type: Article

References (24)

1. Reaven G.M. (1998) Banting lecture: role of insulin resistance in human disease. Diabetes;37:1595-1607.
2. Cooper G.J.S., Willis A.C., Clark A., Turner R.C., Sim R.B., Reid K.B.M. (1987) Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci USA;84:8628-8632.
3. Clark A., Cooper G.J., Lewis C.E., Morris J.F., Willis A.C., Reid K.B.M., Turner R.C. (1987) Islet amyloid formed from diabetes associated peptide may be pathogenic in type-2 diabetes. Lancet;2:231-234.
4. Sanke T., Hanabusa T., Nakano Y., Oki C., Okai K., Nishimura S., Kondo M., Nanjo K. (1991) Plasma islet amyloid polypeptide (amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients. Diabetologia;34:129-132.
5. Jaikaran E.T.A.S., Clark A. (2001) Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology. Biochim Biophys Acta;1537:179-203.
6. Harper J.D., Lansbury P.T. Jr (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of amyloid proteins. Ann Rev Biochem;66:385-407.
7. Hardy J., Selkoe D.J. (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science;297:353-356.
8. Merlini G., Bellotti V. (2003) Molecular mechanisms of amyloidosis. N Engl J Med;349:583-596.
9. Clark A., Nilsson M.R. (2004) Islet amyloid: a complication of islet dysfunction or an aetiological factor in Type 2 diabetes? Diabetologia;47:157-169.
10. Jiang P., Xu W., Mu Y. (2009) Amyloidogenesis abolished by proline substitutions but enhanced by lipid binding. PLoS Comput Biol;5:e1000357. doi:10.1371/journal.pcbi.1000357.
11. Betsholtz C., Christmansson L., Engstrom U., Rorsman F., Svensson V., Johnson K.H., Westermark P. (1989) Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species. FEBS Lett;251:261-264.
12. Liang G., Zhao J., Yu X., Zheng J. (2013) Comparative molecular dynamics study of human islet amyloid polypeptide (IAPP) and rat IAPP oligomers. Biochemistry;52:1089-1100.
13. Chakraborty S., Chatterjee B., Basu S. (2012) A mechanistic insight into the amyloidogenic structure of hIAPP peptide revealed from sequence analysis and molecular dynamics simulation. Biophys Chem;168:1-9.
14. Andrews M.N., Winter R. (2011) Comparing the structural properties of human and rat islet amyloid polypeptide by MD computer simulations. Biophys Chem;156:43-50.
15. Tenidis K., Waldner M., Bernhagen J., Fischle W., Bergmann M., Weber M., Merkle M.L., Voelter W., Brunner H., Kapurniotu A. (2000) Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties. J Mol Biol;295:1055-1071.
16. Wu C., Lei H., Duan Y. (2004) Formation of partially ordered oligomers of amyloidogenic hexapeptide (NFGAIL) in aqueous solution observed in molecular dynamics simulations. Biophys J;87:3000-3009.
17. Nielsen J.T., Bjerring M., Jeppesen M.D., Pedersen R.O., Pedersen J.M., Hein K.L., Vosegaard T., Skrydstrup T., Otzen D.E., Nielsen N.C. (2009) Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy. Angew Chem Int Ed Engl;48:2118-2121.
18. Spoel D.V.D., Lindahl E., Hess B., Groenhof G., Mark A.E., Berendsen H.J. (2005) GROMACS: fast, flexible, and free. J Comput Chem;26:1701-1718.
19. Lindahl E., Hess B., Spoel D.V.D. (2001) GROMACS 3.0: a package for molecular simulation and trajectory analysis. J Mol Model;7:306-317.
20. Hess B., Bekker H., Berendsen H.J.C., Fraaije J. (1997) LINCS: a linear constraint solver for molecular simulations. J Comput Chem;18:1463-1472.
21. Liu F.F., Dong X.Y., He L., Middelberg A.P., Sun Y. (2011) Molecular insight into conformational transition of amyloid β-peptide 42 inhibited by (-)-epigallocatechin-3-gallate probed by molecular simulations. J Phys Chem B;115:11879-11887.
22. Marom M., Safonov R., Amram S., Avneon Y., Nachliel E., Gutman M., Zohary K., Azem A., Tsfadia Y. (2009) Interaction of the Tim44 C-terminal domain with negatively charged phospholipids. Biochemistry;48:11185-11195.
23. Lemkul J.A., Bevan D.R. (2010) Assessing the stability of Alzheimer's amyloid protofibrils using molecular dynamics. J Phys Chem B;114:1652-1660.
24. Kabsch W., Sander C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers;22:2577-2637.