Relevant bibliographies by topics / Insulin hexamer

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Insulin hexamer'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 February 2022

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Journal articles on the topic "Insulin hexamer"

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Shneine, Jewad, Marc Voswinkel, Matthias Federwisch, and Axel Wollmer. "Enhancing the T R Transition of Insulin by Helix-Promoting Sequence Modifications at the N-Terminal B-Chain." Biological Chemistry 381, no. 2 (2000): 127–33. http://dx.doi.org/10.1515/bc.2000.018.

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Abstract Structurally, the T→R transition of insulin mainly consists of a rearrangement of the N-terminal B-chain (residues B1–B8) from extended to helical in one or both of the trimers of the hexamer. The dependence of the transition on the nature of the ligands inducing it, such as inorganic anions or phenolic compounds, as well as of the metal ions complexing the hexamer, has been the subject of extensive investigations. This study explores the effect of helix-enhancing modifications of the N-terminal B-chain sequence where the transition actually occurs, with special emphasis on N-capping. In total 15 different analogues were prepared by semisynthesis. 80% of the hexamers of the most successful analogues with zinc were found to adopt the T3R3 state in the absence of any transforming ligands, as compared to only 4% of wild-type insulin. Transformation with SCN− ions can exceed the T3R3 state where it stops in the case of wild-type insulin. Full transformation to the R6 state can be achieved by only one-tenth the phenol concentration required for wild-type insulin, i. e. almost at the stoichiometric ratio of 6 phenols per hexamer.
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Chang, Xiaoqing, Anne Marie M. Jørgensen, Peter Bardrum, and Jens J. Led. "Solution Structures of the R6Human Insulin Hexamer†,‡." Biochemistry 36, no. 31 (1997): 9409–22. http://dx.doi.org/10.1021/bi9631069.

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Kurtzhals, Peter, Benedicte Kiehr, and Anders R. Sørensen. "The Cobalt(lll)–Insulin Hexamer is a Prolonged‐Acting Insulin Prodrug." Journal of Pharmaceutical Sciences 84, no. 10 (1995): 1164–68. http://dx.doi.org/10.1002/jps.2600841006.

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Wang, D. C., Z. H. Zeng, and Y. L. Hu. "A new structure type of insulin hexamer T3R3t." Acta Crystallographica Section A Foundations of Crystallography 49, s1 (1993): c117. http://dx.doi.org/10.1107/s0108767378096622.

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Lisi, George P., Chien Yi M. Png, and Dean E. Wilcox. "Thermodynamic Contributions to the Stability of the Insulin Hexamer." Biochemistry 53, no. 22 (2014): 3576–84. http://dx.doi.org/10.1021/bi401678n.

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Mukherjee, Saumyak, Ashish A. Deshmukh, Sayantan Mondal, Balasubramanian Gopal, and Biman Bagchi. "Destabilization of Insulin Hexamer in Water–Ethanol Binary Mixture." Journal of Physical Chemistry B 123, no. 49 (2019): 10365–75. http://dx.doi.org/10.1021/acs.jpcb.9b07689.

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Manallack, D. T., P. R. Andrews, and E. F. Woods. "Design, synthesis, and testing of insulin hexamer-stabilizing agents." Journal of Medicinal Chemistry 28, no. 10 (1985): 1522–26. http://dx.doi.org/10.1021/jm00148a025.

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Palmieri, Leonardo C., Maely P. Fávero-Retto, Daniela Lourenço, and Luís Mauricio T. R. Lima. "A T3R3 hexamer of the human insulin variant B28Asp." Biophysical Chemistry 173-174 (March 2013): 1–7. http://dx.doi.org/10.1016/j.bpc.2013.01.003.

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Rimmerman, Dolev, Denis Leshchev, Darren J. Hsu, et al. "Insulin hexamer dissociation dynamics revealed by photoinduced T-jumps and time-resolved X-ray solution scattering." Photochemical & Photobiological Sciences 17, no. 7 (2018): 874–82. http://dx.doi.org/10.1039/c8pp00034d.

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Shoelson, Steven E., Zi Xian Lu, Lina Parlautan, Claire S. Lynch, and Michael A. Weiss. "Mutations at the dimer, hexamer, and receptor-binding surfaces of insulin independently affect insulin-insulin and insulin-receptor interactions." Biochemistry 31, no. 6 (1992): 1757–67. http://dx.doi.org/10.1021/bi00121a025.

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Dissertations / Theses on the topic "Insulin hexamer"

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Bueche, Blaine. "The Effect of PEG-Insulin and Insulin Hexamer Assembly on Stability in Solution and Dry Powders. Hexamer Assembly of PEGylated-Insulin and Insulin Studied by Multi-Angle Light Scattering to Rationally Choose the pH and Zinc Content for Analytical Methods and Formulations of Dry Powders." Thesis, University of Bradford, 2010. http://hdl.handle.net/10454/5688.

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The objective of this research is to further define the relationship between the charge state of insulin, and the self assembly properties of insulin and PEGylated insulin in solution. Polyethylene glycol (PEG) chains were covalently attached to insulin in order to evaluate their impact on insulin's systemic duration of action after pulmonary dosing. This thesis will focus on the assembly properties of the PEG-insulin and insulin, and also demonstrate how the charge state, which was modified by the covalent attachment of PEG, relates to different modes of behavior by anion and cation exchange chromatography. In addition, explain how modifying the assembly state extends to improving formulation properties of spray-dried insulin powders. This thesis is an investigation into the relationship of insulin's charge state controlled by pH and how the charge state affects the self assembly of insulin, especially when the zinc ion is removed. Ionic interaction is one of the major forces affecting insulin assembly. The theory that a change in the charge state of insulin could modulate the ionic interaction and reduce hexamer formation at alkaline conditions was investigated. Experiments were designed to measure the level of hexamer with light scattering, and the amount of hexamer was then correlated with the pH and zinc content of the solutions. The importance of the charge state of the monomer and its behavior extends to chromatography and purification modes as well. Specifically, the purification of various species of PEGylated insulin presents a challenge. By varying mobile phase pH which induces the charge to insulin, an ion exchange method demonstrated very high resolution and controllable interaction between the ion exchange media and the insulin derivatives. A highly accurate method for determining molecular weight and thus the average associated state of insulin in solution has been developed using the MALS (Multi-Angle Light Scattering). Insulin concentration, pH, and metal ion concentrations, were in pharmaceutically relevant ranges. The MALS method was developed to evaluate how the parameters above affect the self-assembly properties of insulin, and use the assembly properties to improve formulations of insulin or PEGylated insulin. To use the light scattering technique the dn/dc (change in refractive index with change in concentration) is required. During the method development, the dn/dc of insulin was measured at 690 nm, and a value of 0.185 mL/g based on theory was confirmed. A novel approach for preparing insulin powders with improved chemical stability, based on maintaining the dissociation of hexamers in solution during the spray drying process was developed. The mode presented here is to remove the zinc ions from solution, increase the pH from 6.6 to 7.8, and maintain a low concentration of insulin approximately 2 to 15 mg/mL. Each of these factors alone decreases the hexamer population in solution, but by combining all three factors, hexamers are driven to very low levels of equilibrium. The increased stability of the powders is predominately related to the decrease in covalent insulin dimer (CID). The data presented correlates a reduced hexamer population in the solution with lower levels of CID's in the dry powder compared to controls. The CID formation rate was reduced by 40% compared to a control.
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Whittingham, Jean Lesley. "Ligand binding in hexameric insulins." Thesis, University of York, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.385408.

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Derewenda, Urszula. "X-ray analysis of dimeric and hexameric insulins." Thesis, University of York, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.276517.

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Gao, Quan-Ze, and 高銓澤. "An Improvement of the Biomolecular Free Energy Calculation: Conformational Change in Insulin Hexamer." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/e3ahc2.

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Palivec, Vladimír. "Počítačové modelování interakcí iont ů s proteiny: Allosterický efekt iont ů a fenolických ligand ů na strukturu insulinového hexameru." Master's thesis, 2016. http://www.nusl.cz/ntk/nusl-344126.

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Title: Computer modeling of ion protein interactions: Allosteric effects of phenolic ligands and ions on insulin hexamer structure Author: Vladimír Palivec Department: Department of Physical and Macromolecular Chemistry Faculty of Science UK Advisor: prof. RNDr. Pavel Jungwirth, DSc., IOCB AS CR, v.v.i. Advisor's email address: pavel.jungwirth@uochb.cas.cz Abstract: Insulin hexamer is an allosteric protein capable of undergoing conformational changes between three states: T6, T3R3, and R6. Transitions between them, as well as the formation of insulin hexamers, are mediated through binding of phenolic ligands or ions. This thesis presents a molecular dynamics study of allosteric behavior of insulin using empirical force fields. Two effects are closely inspected - cation (Zn2+ , Ca2+ , K+ , and Na+ ) binding to the insulin hexamers and a possible binding of two neurotransmitters - dopamine and serotonin to the phenolic pocket. The results show that high charge density cations (Zn2+ and Ca2+ ) are mostly localized in the B13 glutamate cavity, slow- down diffusion, while preventing other cations from entering. In contrast, low charge density cations (Na+ and K+ ) do not have this effect. Concerning neurotransmitters, dopamine does not bind to the phenolic pocket whereas serotonin binds in a similar way like...
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Mroue, Kamal. "Solid-State NMR Investigations of 67Zn and 27Al Nuclei in Zinc-Amino Acid Complexes, Zinc-Insulin Hexamers, and Aluminum-Centered Dyes." Thesis, 2010. http://hdl.handle.net/10012/5018.

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Modern solid-state nuclear magnetic resonance (NMR) methodologies are applied to investigate two spin-5/2 nuclei, Zn-67 and Al-27, in different coordination environments in order to characterize the magnitudes and orientations of their electric field gradient (EFG) and nuclear magnetic shielding tensors. The advantages of using high (21.1 T) applied magnetic fields for detecting Zn-67 directly at ambient temperatures, using the quadrupolar Carr-Purcell Meiboom-Gill (QCPMG) pulse sequence and the stepped-frequency technique, are demonstrated by the successful investigation of the different zinc sites in several zinc-amino acid coordination compounds, and in the more complex polymorphs of the zinc-insulin hexamers. In all systems, the high-field Zn-67 NMR spectra are dominated only by the quadrupolar interaction. The first two Zn-67 NMR spectra of pentacoordinated zinc sites are reported and analyzed. The experimental results are corroborated by ab initio and density functional theory (DFT) calculations of the Zn-67 NMR parameters in order to gain better understanding of the zinc local electronic environments. Solid-state Al-27 NMR is applied to study three commercial aluminum-phthalocyanine dyes. Solid-state Al-27 NMR experiments, including multiple-quantum magic-angle-spinning (MQMAS) and quadrupolar Carr-Purcell Meiboom-Gill (QCPMG), are employed at multiple high magnetic field strengths (11.7, 14.1 and 21.1 T) to determine the composition and number of aluminum distinct sites in these dyes. The quadrupolar parameters for each Al-27 site are determined from spectral simulations, with quadrupolar coupling constants ranging from 5.40 to 10.0 MHz and asymmetry parameters ranging from 0.10 to 0.50, and compare well with the results of quantum chemical calculations of these tensors. The largest Al-27 chemical shielding anisotropy (CSA), with a span of 120 ppm, observed directly in a solid material is also reported. The combination of MQMAS and computational chemistry are used to interpret the presence of multiple aluminum sites in two of the three samples.
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Book chapters on the topic "Insulin hexamer"

1

Kurtzhals, P., U. Ribel, L. Schäffer, and N. C. Kaarsholm. "Co3+-insulin hexamer is a prodrug of human insulin." In Peptides 1994. Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-1468-4_405.

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Smith, G. D., D. C. Swenson, Z. Derewenda, et al. "The structure of a new hexameric form of human insulin." In Peptides. Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-010-9595-2_10.

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3

Dunn, Michael F., Richard Palmieri, Niels C. Kaarsholm, et al. "THE 2-ZINC INSULIN HEXAMER IS A CALCIUM-BINDING PROTEIN." In Calcium-Binding Proteins in Health and Disease. Elsevier, 1987. http://dx.doi.org/10.1016/b978-0-12-521040-9.50062-0.

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Journal articles
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