Jentashapir Journal of Health Research

Published by: Kowsar

Temperature and pH Effects on Insulin Structure: A Molecular Dynamic Approach

Mahboubeh Baheri 1 and Mohammad Reza Dayer 1 , *
Authors Information
1 Biology Department, Shahid Chamran University of Ahvaz, Ahvaz, IR Iran
Article information
  • Jentashapir Journal of Health Research: August 01, 2016, 7 (4); e36931
  • Published Online: August 28, 2016
  • Article Type: Research Article
  • Received: February 6, 2016
  • Revised: April 18, 2016
  • Accepted: May 27, 2016
  • DOI: 10.17795/jjhr-36931

To Cite: Baheri M, Dayer M R. Temperature and pH Effects on Insulin Structure: A Molecular Dynamic Approach, Jentashapir J Health Res. 2016 ; 7(4):e36931. doi: 10.17795/jjhr-36931.

Copyright © 2016, Ahvaz Jundishapur University of Medical Sciences. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International License ( which permits copy and redistribute the material just in noncommercial usages, provided the original work is properly cited.
1. Background
2. Objectives
3. Methods
4. Results
5. Discussion
  • 1. Definition, Diagnosis and Classification of Diabetes Mellitus and its Complications. Part 1: Diagnosis and Classification of Diabetes Mellitus. 1999;
  • 2. Hjorth CF, Norrman M, Wahlund PO, Benie AJ, Petersen BO, Jessen CM, et al. Structure, Aggregation, and Activity of a Covalent Insulin Dimer Formed During Storage of Neutral Formulation of Human Insulin. J Pharm Sci. 2016; 105(4): 1376-86[DOI][PubMed]
  • 3. Vinther TN, Norrman M, Ribel U, Huus K, Schlein M, Steensgaard DB, et al. Insulin analog with additional disulfide bond has increased stability and preserved activity. Protein Sci. 2013; 22(3): 296-305[DOI][PubMed]
  • 4. Vinther TN, Pettersson I, Huus K, Schlein M, Steensgaard DB, Sorensen A, et al. Additional disulfide bonds in insulin: Prediction, recombinant expression, receptor binding affinity, and stability. Protein Sci. 2015; 24(5): 779-88[DOI][PubMed]
  • 5. Li Y, Gong H, Sun Y, Yan J, Cheng B, Zhang X, et al. Dissecting the role of disulfide bonds on the amyloid formation of insulin. Biochem Biophys Res Commun. 2012; 423(2): 373-8[DOI][PubMed]
  • 6. Mishra NK, Joshi KB, Verma S. Inhibition of human and bovine insulin fibril formation by designed peptide conjugates. Mol Pharm. 2013; 10(10): 3903-12[DOI][PubMed]
  • 7. Choi JH, May BC, Wille H, Cohen FE. Molecular modeling of the misfolded insulin subunit and amyloid fibril. Biophys J. 2009; 97(12): 3187-95[DOI][PubMed]
  • 8. Hong Y, Meng L, Chen S, Leung CW, Da LT, Faisal M, et al. Monitoring and inhibition of insulin fibrillation by a small organic fluorogen with aggregation-induced emission characteristics. J Am Chem Soc. 2012; 134(3): 1680-9[DOI][PubMed]
  • 9. Cheng B, Gong H, Xiao H, Petersen RB, Zheng L, Huang K. Inhibiting toxic aggregation of amyloidogenic proteins: a therapeutic strategy for protein misfolding diseases. Biochim Biophys Acta. 2013; 1830(10): 4860-71[DOI][PubMed]
  • 10. Ratanji KD, Derrick JP, Dearman RJ, Kimber I. Immunogenicity of therapeutic proteins: influence of aggregation. J Immunotoxicol. 2014; 11(2): 99-109[DOI][PubMed]
  • 11. Fodera V, Librizzi F, Groenning M, van de Weert M, Leone M. Secondary nucleation and accessible surface in insulin amyloid fibril formation. J Phys Chem B. 2008; 112(12): 3853-8[DOI][PubMed]
  • 12. Whittingham JL, Scott DJ, Chance K, Wilson A, Finch J, Brange J, et al. Insulin at pH 2: structural analysis of the conditions promoting insulin fibre formation. J Mol Biol. 2002; 318(2): 479-90[DOI][PubMed]
  • 13. Ivanova MI, Sievers SA, Sawaya MR, Wall JS, Eisenberg D. Molecular basis for insulin fibril assembly. Proc Natl Acad Sci U S A. 2009; 106(45): 18990-5[DOI][PubMed]
  • 14. Pedersen JT, Heegaard NH. Analysis of protein aggregation in neurodegenerative disease. Anal Chem. 2013; 85(9): 4215-27[DOI][PubMed]
  • 15. Weiss MA. The structure and function of insulin: decoding the TR transition. Vitam Horm. 2009; 80: 33-49[DOI][PubMed]
  • 16. Dayer MR, Azari N, Razmi N, Dayer MS. The Effects of Temperature Changes on Human Prion Protein Conformation Using Molecular Dynamic Simulation. Arak Med Univ J. 2014; 17(88): 48-58
  • 17. Scopes RK. Protein purification: principles and practice. 2013;
  • 18. Herczenik E, Gebbink MF. Molecular and cellular aspects of protein misfolding and disease. FASEB J. 2008; 22(7): 2115-33[DOI][PubMed]
  • 19. Ksenofontova OI, Romanovskaya EV, Stefanov VE. [Study of conformational mobility of insulin, proinsulin, and insulin-like growth factors]. Zh Evol Biokhim Fiziol. 2014; 50(1): 38-43[PubMed]
  • 20. Smith MI, Fodera V, Sharp JS, Roberts CJ, Donald AM. Factors affecting the formation of insulin amyloid spherulites. Colloids Surf B Biointerfaces. 2012; 89: 216-22[DOI][PubMed]
  • 21. Kachooei E, Moosavi-Movahedi AA, Khodagholi F, Ramshini H, Shaerzadeh F, Sheibani N. Oligomeric forms of insulin amyloid aggregation disrupt outgrowth and complexity of neuron-like PC12 cells. PLoS One. 2012; 7(7)[DOI][PubMed]
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