Application of SIMSTEX to Oligomerization of Insulin Analogs and Mutants

Journal of the American Society for Mass Spectrometry

Volumn 17, Issue 11, 2006, Pages 1526-1534

  Chitta, Raghu K ^a   Rempel, Don L ^a   Grayson, Michael A ^a   Remsen, Edward E ^a   Gross, Michael L ^a  

^a WASHINGTON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DEUTERIUM; INSULIN; MASS SPECTROMETRY; MUTAGENESIS; NITROGEN COMPOUNDS; POLYMERIZATION; PROTEINS; TITRATION;

AFFINITY CONSTANTS; DIABETES; MUTANTS; OLIGOMERIZATION;

OLIGOMERS;

AMIDE; BOVINE INSULIN; DEUTERIUM; HYDROGEN; INSULIN DERIVATIVE; INSULIN LISPRO; LIGAND; OLIGOMER; PIG INSULIN; PROTEIN; RECOMBINANT HUMAN INSULIN;

ANALYTIC METHOD; ARTICLE; BINDING AFFINITY; DEUTERIUM HYDROGEN EXCHANGE; DRUG DETERMINATION; GAS; LIGAND BINDING; MASS SPECTROMETRY; OLIGOMERIZATION; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN STRUCTURE; SELF ASSOCIATION INTERACTIONS USING MASS SPECTROMETRY SELF TITRATION AND HYDROGEN DEUTERIUM EXCHANGE; TITRIMETRY;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; DEUTERIUM EXCHANGE MEASUREMENT; HUMANS; HYDROGEN; INSULIN; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SWINE;

EID: 33750353889     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2006.08.004     Document Type: Article

References (35)

1. Brange J., and Langkjoer L. Insulin Structure and Stability. Pharm. Biotech. 5 (1993) 315-350
2. DeFelippis M.R., Chance R.E., and Frank B.H. Insulin Self-Association and the Relationship to Pharmacokinetics and Pharmacodynamics. Crit. Rev. Therap. Drug. Carrier Sys. 18 (2001) 201-264
3. Brange J., and Volund A. Insulin Analogs with Improved Pharmacokinetic Profiles. Adv. Drug Delivery Rev. 35 (1999) 307-335
4. Kang S., Brange J., Burch A., Volund A., and Owens D.R. Subcutaneous Insulin Absorption Explained by Insulin's Physicochemical Properties. Evidence from Absorption Studies of Soluble Human Insulin and Insulin Analogs in Humans. Diabetes Care 14 (1991) 942-948
5. Holleman F., and Hoekstra J.B.L. Insulin Analogs: The Virtual Reality of Normal Insulin Secretion. Nether. J. Med. 47 (1995) 95-98
6. Markussen J., Diers I., Engesgaard A., Hansen M.T., Hougaard P., Langkjaer L., Norris K., Ribel U., and Soerensen A.R. Soluble, Prolonged-Acting Insulin Derivatives. II. Degree of Protraction and Crystallizability of Insulins Substituted in Positions A17, B8, B13, B27, and B30. Protein Eng. 1 (1987) 215-223
7. Brems D.N., Alter L.A., Beckage M.J., Chance R.E., DiMarchi R.D., Green L.K., Long H.B., Pekar A.H., Shields J.E., and Frank B.H. Altering the Association Properties of Insulin by Amino Acid Replacement. Protein Eng. 5 (1992) 527-533
8. Pillai O., and Panchagnula R. Insulin Therapies-Past, Present, and Future. Drug Discovery Today 6 (2001) 1056-1061
9. Holleman F., and Hoekstra J.B.L. Insulin Lispro. N. Engl. J. Med. 337 (1997) 176-183
10. Blundell T., Dodson G., Hodgkin D., and Mercola D. Insulin Structure in the Crystal and Its Reflection in Chemistry and Biology. Adv. Protein Chem. 26 (1972) 279-402
11. Baker E.N., Blundell T.L., Cutfield J.F., Cutfield S.M., Dodson E.J., Dodson G.G., Hodgkin D.M., Hubbard R.E., Isaacs N.W., and Reynolds C.D. The Structure of 2Zn Pig Insulin Crystals at 1.5 A Resolution. Philosophical Transactions of the Royal Society of London 319 (1988) 369-456
12. Slieker L.J., Brooke G.S., DiMarchi R.D., Flora D.B., Green L.K., Hoffmann J.A., Long H.B., Fan L., Schields J.E., Sundell K.L., Surface O.L., and Chance R.E. Modifications in the B10 and B26-30 Regions of the B Chain of Human Insulin Alter Affinity for the Human IGF-I Receptor More than for the Insulin Receptor. Diabetologia 40 (1997) S54-S61
13. Bentley G.A., Brange J., Derewenda Z., Dodson E.J., Dodson G.G., Markussen J., Wilkinson A.J., Wollmer A., and Xiao B. Role of B13 Glu in Insulin Assembly. The Hexamer Structure of Recombinant Mutant (B13 Glu - > Gln) Insulin. J. Mol. Biol. 228 (1992) 1163-1176
14. Ramanathan R., Gross M.L., Zielinski W.L., and Layloff T.P. Monitoring Recombinant Protein Drugs: A Study of Insulin by H/D Exchange and Electrospray Ionization Mass Spectrometry. Anal. Chem. 69 (1997) 5142-5145
15. Zhu M.M., Rempel D.L., Zhao J., Giblin D.E., and Gross M.L. Probing Ca2+ Induced Conformational Changes in Porcine Calmodulin by H/D Exchange and ESI-MS: Effect of Cations and Ionic Strength. Biochemistry 42 (2003) 15388-15397
16. Zhang Z., and Smith D.L. Determination of Amide Hydrogen Exchange by Mass Spectrometry: A New Tool for Protein Structure Elucidation. Protein Sci. 2 (1993) 522-531
17. Engen J.R., and Smith D.L. Investigating Protein Structure and Dynamics by Hydrogen Exchange MS. Anal. Chem. 73 (2001) 256A-265A
18. Eyles S.J., Gumerov D.R., Gierasch L.M., and Kaltashov I.A. Probing Protein Folding and Binding by Electrospray Ionization Fourier Transform Mass Spectrometry. Adv. Mass Spectrom. 15 (2001) 499-500
19. Mandell J.G., Baerga-Ortiz A., Akashi S., Takio K., and Komives E.A. Solvent Accessibility of the Thrombin-Thrombomodulin Interface. J. Mol. Biol. 306 (2001) 575-589
20. Komives E.A. Protein-Protein Interaction Dynamics by Amide H/H-2 Exchange Mass Spectrometry. Int. J. Mass Spectrom. 240 (2005) 285-290
21. Powell K.D., Ghaemmaghami S., Wang M.Z., Ma L., Oas T.G., and Fitzgerald M.C. A General Mass Spectrometry-Based Assay for the Quantitation of Protein-Ligand Binding Interactions in Solution. J. Am. Chem. Soc. 124 (2002) 10256-10257
22. Zhu M.M., Rempel D.L., Du Z., and Gross M.L. Quantification of Protein-Ligand Interactions by Mass Spectrometry, Titration, and H/D Exchange: PLIMSTEX. J. Am. Chem. Soc. 125 (2003) 5252-5253
23. Zhu M.M., Rempel D.L., and Gross M.L. Modeling Data from Titration, Amide H/D Exchange, and Mass Spectrometry to Obtain Protein-Ligand Binding Constants. J. Am. Soc. Mass Spectrom. 15 (2004) 388-397
24. Chitta R.K., Rempel D.L., and Gross M.L. Determination of Affinity Constants and Response Factors of the Noncovalent Dimer of Gramicidin by Electrospray Ionization Mass Spectrometry and Mathematical Modeling. J. Am. Soc. Mass Spectrom. 16 (2005) 1031-1038
25. Johnson M.L. Why, When, and How Biochemists Should Use Least Squares. Anal. Biochem. 206 (1992) 215-225
26. Kadima W., Oegendal L., Bauer R., Kaarsholm N., Brodersen K., Hansen J.F., and Porting P. The Influence of Ionic Strength and pH on the Aggregation Properties of Zinc-Free Insulin Studied by Static and Dynamic Laser Light Scattering. Biopolymers 33 (1993) 1643-1657
27. Nettleton E.J., Tito P., Sunde M., Bouchard M., Dobson C.M., and Robinson C.V. Characterization of the Oligomeric States of Insulin in Self-Assembly and Amyloid Fibril Formation by Mass Spectrometry. Biophys. J. 79 (2000) 1053-1065
28. Pocker Y., and Biswas S.B. Self-Association of Insulin and the Role of Hydrophobic Bonding: A Thermodynamic Model of Insulin Dimerization. Biochemistry 20 (1981) 4354-4361
29. Praissman M., and Rupley J.A. Comparison of Protein Structure in the Crystal and in Solution. II. Tritium-Hydrogen Exchange of Zinc-Free and Zinc Insulin. Biochemistry 7 (1968) 2431-2445
30. Pekar A.H., and Frank B.H. Conformation of Proinsulin. Comparison of Insulin and Proinsulin Self-Association at Neutral pH. Biochemistry 11 (1972) 4013-4016
31. Holladay L.A., Ascoli M., and Puett D. Conformational Stability and Self-Association of Zinc-Free Bovine Insulin at Neutral pH. Biochim. Biophys. Acta. 494 (1977) 245-254
32. Markussen J., Diers I., Hougaard P., Langkjaer L., Norris K., Snel L., Soerensen A.R., Soerensen E., and Voigt H.O. Soluble, Prolonged-Acting Insulin Derivatives. II. Degree of Protraction, Crystallizability, and Chemical Stability of Insulins Substituted in Positions A21, B13, B23, B27, and B30. Protein Eng. 2 (1988) 157-166
33. Volund A., Brange J., Drejer K., Jensen I., Markussen J., Ribel U., Sorensen A.R., and Schlichtkrull J. In Vitro and in Vivo Potency of Insulin Analogs Designed for Clinical Use. Diabetic Med. 8 (1991) 839-847
34. Jorgensen A.M., Kristensen S.M., Led J.J., and Balschmidt P. Three-Dimensional Solution Structure of an Insulin Dimer. A Study of the B9(Asp) Mutant of Human Insulin Using Nuclear Magnetic Resonance, Distance Geometry, and Restrained Molecular Dynamics. J. Mol. Biol. 227 (1992) 1146-1163
35. Wang S.H., Hu S.Q., Burke G.T., and Katsoyannis P.G. Insulin Analogs with Modifications in the β-Turn of the B-chain. J. Protein Chem. 10 (1991) 313-324