Search results for: Ramil F. Latypov

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Free Fatty Acid Particles in Protein Formulations, Part 2: Contribution of Polysorbate Raw Material

Christine C. Siska, Christopher J. Pierini, Hollis R. Lau, Ramil F. Latypov, more

Journal of Pharmaceutical Sciences > 104 > 2 > 447 - 456

Polysorbate 20 (PS20) is a nonionic surfactant frequently used to stabilize protein biopharmaceuticals. During the development of mAb formulations containing PS20, small clouds of particles were observed in solutions stored in vials. The degree of particle formation was dependent on PS20 concentration. The particles were characterized by reversed‐phase HPLC after dissolution and labeling with the...

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Banks DD, Latypov RF, Ketchem RR, Woodard J, Scavezze JL, Siska CC, Razinkov VI. 2012. Native‐State Solubility and Transfer Free Energy as Predictive Tools for Selecting Excipients to Include in Protein Formulation Development Studies. J Pharm Sci 101:2720–2732.

Douglas D. Banks, Ramil F. Latypov, Randal R. Ketchem, Jon Woodard, more

Journal of Pharmaceutical Sciences > 102 > 3 > 1137 - 1138

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Native‐state solubility and transfer free energy as predictive tools for selecting excipients to include in protein formulation development studies

Douglas D. Banks, Ramil F. Latypov, Randal R. Ketchem, Jon Woodard, more

Journal of Pharmaceutical Sciences > 101 > 8 > 2720 - 2732

In the present report, two formulation strategies, based on different aggregation models, were compared for their ability to quickly predict which excipients (cosolutes) would minimize the aggregation rate of an immunoglobulin G1 monoclonal antibody (mAb‐1) stored for long term at refrigerated and room temperatures. The first formulation strategy assumed that a conformational change to an aggregation‐prone...

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Effect of benzyl alcohol on recombinant human interleukin‐1 receptor antagonist structure and hydrogen–deuterium exchange

John R. Alford, Andrew C. Fowler, Deborah S. Wuttke, Bruce A. Kerwin, more

Journal of Pharmaceutical Sciences > 100 > 10 > 4215 - 4224

Benzyl alcohol, a preservative commonly added to multidose therapeutic protein formulations, can accelerate aggregation of recombinant human interleukin‐1 receptor antagonist (rhIL‐1ra). To investigate the interactions between benzyl alcohol and rhIL‐1ra, we used nuclear magnetic resonance to observe the effect of benzyl alcohol on the chemical shifts of amide resonances of rhIL‐1ra and to measure...

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Acid-Induced Aggregation of Human Monoclonal IgG1 and IgG2: Molecular Mechanism and the Effect of Solution Composition

Sanjay B. Hari, Hollis Lau, Vladimir I. Razinkov, Shuang Chen, more

Biochemistry > 2010 > 49 > 43 > 9328 - 9338

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Characterization of a unique IgG1 mAb CEX profile by limited Lys-C proteolysis/CEX separation coupled with mass spectrometry and structural analysis

Jaewon Kim, Laurie Jones, Lisa Taylor, Gunasekaran Kannan, more

Journal of Chromatography B > 2010 > 878 > 22 > 1973-1981

The unique cation exchange chromatography (CEX) charge variant profile of mAb1 is characterized by a combination of mass spectrometry, limited Lys-C digestion followed by CEX separation and structural analysis. During CEX method development, mAb1 showed several unexpected phenomena, including a unique profile containing two main species (acidic 2 and main) and significant instability during stability...

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Investigation of degradation processes in IgG1 monoclonal antibodies by limited proteolysis coupled with weak cation-exchange HPLC

Hollis Lau, Danielle Pace, Boxu Yan, Theresa McGrath, more

Journal of Chromatography B > 2010 > 878 > 11-12 > 868-876

A new cation-exchange high-performance liquid chromatography (HPLC) method that separates fragment antigen-binding (Fab) and fragment crystallizable (Fc) domains generated by the limited proteolysis of monoclonal antibodies (mAbs) was developed. This assay has proven to be suitable for studying complex degradation processes involving various immunoglobulin G1 (IgG1) molecules. Assignment of covalent...

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High throughput thermostability screening of monoclonal antibody formulations

Feng He, Sabine Hogan, Ramil F. Latypov, Linda O. Narhi, more

Journal of Pharmaceutical Sciences > 99 > 4 > 1707 - 1720

Differential scanning fluorimetry (DSF) was employed to increase the throughput of the thermostability screening of monoclonal antibody (mAb) formulations. The method consists of measuring the fluorescence intensity of a polarity sensitive probe at gradually increasing temperatures, and obtaining the transition temperature of exposure of the hydrophobic regions of proteins (T_h). The change in fluorescence...

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Denaturant-Dependent Conformational Changes in a β-Trefoil Protein: Global and Residue-Specific Aspects of an Equilibrium Denaturation Process

Ramil F. Latypov, Dingjiang Liu, Jaby Jacob, Timothy S. Harvey, more

Biochemistry > 2009 > 48 > 46 > 10934 - 10947

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Folding Mechanism of Reduced Cytochrome c: Equilibrium and Kinetic Properties in the Presence of Carbon Monoxide

Ramil F. Latypov, Kosuke Maki, Hong Cheng, Stanley D. Luck, more

Journal of Molecular Biology > 2008 > 383 > 2 > 437-453

Despite close structural similarity, the ferric and ferrous forms of cytochrome c differ greatly in terms of their ligand binding properties, stability, folding, and dynamics. The reduced heme iron binds diatomic ligands such as CO only under destabilizing conditions that promote weakening or disruption of native methionine–iron linkage. This makes CO a useful conformational probe for detecting partially...

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Proapoptotic activity of cytochrome c in living cells: effect of K72 substitutions and species differences

Rita V. Chertkova, George V. Sharonov, Alexei V. Feofanov, Ol’ga V. Bocharova, more

Molecular and Cellular Biochemistry > 2008 > 314 > 1-2 > 85-93

Cytochrome c is one of the key proteins involved in the programmed cell death, and lysine 72 is known to be required for its apoptogenic activity. We have engineered a number of horse and murine cytochrome c single-point mutants with various substitutions at position 72 and compared quantitatively their proapoptotic activity in living cells. Apoptosis was activated by transferring exogenous cytochrome...

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Biophysical Characterization of Structural Properties and Folding of Interleukin-1 Receptor Antagonist

Ramil F. Latypov, Timothy S. Harvey, Dingjiang Liu, Pavel V. Bondarenko, more

Journal of Molecular Biology > 2007 > 368 > 4 > 1187-1201

Structural properties and folding of interleukin-1 receptor antagonist (IL-1ra), a therapeutically important cytokine with a symmetric β-trefoil topology, are characterized using optical spectroscopy, high-resolution NMR, and size-exclusion chromatography. Spectral contributions of two tryptophan residues, Trp17 and Trp120, present in the wild-type protein, have been determined from mutational analysis...

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Conformational Equilibration Time of Unfolded Protein Chains and the Folding Speed Limit ^†

Christina J. Abel, Robert A. Goldbeck, Ramil F. Latypov, Heinrich Roder, more

Biochemistry > 2007 > 46 > 13 > 4090 - 4099

article

Structural Characterization of an Equilibrium Unfolding Intermediate in Cytochrome c

Ramil F. Latypov, Hong Cheng, Navid A. Roder, Jiaru Zhang, more

Journal of Molecular Biology > 2006 > 357 > 3 > 1009-1025

Although the denaturant-induced unfolding transition of cytochrome c was initially thought to be a cooperative process, recent spectroscopic studies have shown deviations from two-state behavior consistent with accumulation of an equilibrium intermediate. However, little is known about the structural and thermodynamic properties of this state, and whether it is stabilized by the presence of non-native...

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Anion Binding and Controlled Aggregation of Human Interleukin-1 Receptor Antagonist

Andrei A. Raibekas, Edward J. Bures, Christine C. Siska, Tadahiko Kohno, more

Biochemistry > 2005 > 44 > 29 > 9871 - 9879

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Rapid Intrachain Binding of Histidine-26 and Histidine-33 to Heme in Unfolded Ferrocytochrome c ^†

Stephen J. Hagen, Ramil F. Latypov, Dimitry A. Dolgikh, Heinrich Roder

Biochemistry > 2002 > 41 > 4 > 1372 - 1380

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Structure and stability of recombinant protein depend on the extra N-terminal methionine residue: S6 permutein from direct and fusion expression systems

Vladimir N. Uversky, Ziedulla Kh. Abdullaev, Alexander S. Arseniev, Eduard V. Bocharov, more

Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology > 1999 > 1432 > 2 > 324-332

Two permuted variants of S6 ribosomal protein were obtained in direct and fusion expression systems, respectively. The product of direct expression contained the extra N-terminal methionine residue. The structural properties and conformational stability of these permuteins were compared using 1-D ¹ H-NMR, circular dichroism, intrinsic fluorescence, differential scanning calorimetry and resistance...

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S6 permutein shows that the unusual target topology is not responsible for the absence of rigid tertiary structure in de novo protein albebetin

Ziedulla Kh. Abdullaev, Ramil F. Latypov, Azat Ya. Badretdinov, Dmitry A. Dolgikh, more

FEBS Letters > 1997 > 414 > 2 > 243-246

Ribosomal protein S6 from Thermus thermophilus was modified to form the unusual unique topology designed earlier for a de novo protein albebetin. The S6 gene was cloned, sequenced and circularly permutated by means of genetic engineering methods. The permutated gene was expressed in Escherichia coli and the permutein was isolated and investigated by means of circular dichroism, fluorescence spectroscopy...

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