Untitled

Anisimova, M. V.; Shulga, A. A.; Levichkin, Iliya V; Кирпичников, М. П.; Polyakov, K. M.; Skryabin, K. G.; Vijayalakshmi, M.A.; Варламов, В. П.

doi:10.1023/a:1009522917352

Cited by 4 publications

(4 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Expression plasmids for GHs were constructed by replacement of gene 10 in pGEMEX1 (Promega) with a GH gene [2]. Proteins were purified from the Escherichia coli strain BL21(DE3) harboring the corresponding expression plasmid [7].…”

Section: Methodsmentioning

confidence: 99%

Increased stability of human growth hormone with reduced lactogenic potency

et al. 2002

View full text Add to dashboard Cite

Human growth hormone (hGH), whose main function is the somatic growth stimulation, induces diverse e¡ects including lactation. We examined the possibility of hGH stabilization by elimination of its lactogenic activity. Chimeric GHs were constructed by replacement of di¡erent segments of hGH with sequences derived from non-lactogenic porcine GH. As was observed in the rat Nb2-11C lymphoma cell test, lactogenic activity of some chimeric hormones was seriously destroyed. This kind of hormones displayed the substantial increase in thermal and guanidine hydrochloride stability. The more stable hGH variants were found to be more soluble in Escherichia coli cells. ß 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

show abstract

Section: Methodsmentioning

confidence: 99%

Increased stability of human growth hormone with reduced lactogenic potency

et al. 2002

View full text Add to dashboard Cite

show abstract

“…IMAGE technique was also applied to study the change of the surface histidines topography of RNase A when chemically glycosylated on exposed carboxylic groups with glucosamine using carbodiimide as cross-linker, under mild conditions [65]. The Zn(II) binding region in growth hormone was studied using IMAGE by Anisimove et al [66]. Using IMAGE structural study of natural and chemically induced oligomeric ribonucleases was done to study the relationship between surface histidine topography in oligomeric forms of these ribonucleases and their catalytic properties [67].…”

Section: Immobilized Metal-ion Affinity Gel Electrophoresismentioning

confidence: 99%

“…This in turn can give information about the structural differences resulting in different functional properties. Structural study and the structure-function relationship of natural and chemical induced oligomeric ribonuclease were also studied using IMACE [66]. Effects of chemical glycosylation with glucosamine of bovine α-chymotrypsin on its catalytic and structural properties, particularly their modification of the affinity for the transition-metal chelate, IDA-Cu(II) was studied by Jiang et al [70] using IMACE.…”

Section: Immobilized Metal-ion Affinity Capillary Electrophoresismentioning

confidence: 99%

Immobilized metal-ion affinity systems for recovery and structure–function studies of proteins at molecular, supramolecular, and cellular levels

Prasanna

Vijayalakshmi

2010

Pure and Applied Chemistry

View full text Add to dashboard Cite

Immobilized metal-ion affinity (IMA) adsorption is a collective term that is used to include all kinds of adsorptions where the metal ion serves as the characteristic and most essential part of adsorption center. Of all the IMA techniques, immobilized metal-affinity chromato graphy (IMAC) has been gaining popularity as the choice of purification technique for proteins. IMAC represents a separation technique that is primarily useful for proteins with natural surface exposed-histidine residues and for recombinant proteins with engineered histidine tag. This review also gives insight into other nonchromatographic applications of IMA adsorption such as immobilized metal-ion affinity gel electrophoresis (IMAGE), immobilized metal-ion affinity capillary electrophoresis (IMACE), and immobilized metal-ion affinity partitioning (IMAP).Keywords: immobilized metal-affinity chromato graphy; immobilized metal-ion affinity capillary electrophoresis; immobilized metal-ion affinity gel electrophoresis; immobilized metal-ion affinity partitioning; metal affinity; proteins.IMA adsorption is a collective term that is used to include all kinds of adsorptions where a metal ion, with affinity for analytes in the sample to be fractionated, is fixed to an insoluble matrix. The metal ion is immobilized to a solid support matrix via coordinate bonding with chelating agent. The metal ion serves as the characteristic and most essential part of the adsorption center [4]. Protein adsorption is based on coordinate bond formation between the immobilized metal ion and the electron donor group from the protein surface.Most commonly used are the transition-metal ions Cu(II), Ni(II), Zn(II), Co(II), Fe(III), which are electron-pair acceptors and can be considered as Lewis acids. Electron-donor atoms (N, S, O) present in the chelating compounds that are immobilized to the chromatographic support are capable of coordinating metal ions and forming metal chelates, which can be bidentate, tridentate, etc., depending on the number of occupied coordination bonds. The remaining metal coordination sites are normally occupied by water molecules and can be exchanged with suitable electron-donor groups from the protein.In addition to the amino terminus, side chains of certain amino acids bind to the chelated metal, due to their electron-donor atoms. Although many residues, such as Glu, Asp (-ve interaction) Tyr, Cys, His, Arg, Lys, and Met (+ve interaction), can interact with the protein, retention in IMAC is based primarily on the availability of histidyl residues under certain pH and ionic conditions. Free cysteines that could also contribute to binding to chelated metal ions are rarely available in the appropriate, reduced state. However, aromatic side chains of Trp, Phe, and Tyr appear to contribute to retention, if they are in the vicinity of accessible histidine residues [8]. Furthermore, the systematic investigation by E. Sulkowski using model homologous series of proteins showed that histidine, a member of Porath's triad (histidine, tryptophan, and cys...

show abstract

“…The variable X residue was positioned in the middle of the peptide to best represent the characteristics of a midchain amino acid in a protein by positioning it relatively far from the zwitterionic end groups. In this initial set of adsorption studies, three different types of amino acids were used for the X residue to vary the overall characteristics of the peptides, with X represented by either threonine (T; -CH(CH 3 )OH side chain, polar character), aspartic acid (D; -CH 2 COOH side chain, negatively charged, p K = 3.9 ), or valine (V; -CH(CH 3 ) 2 side chain, nonpolar character). Each of these three peptides was synthesized and characterized by analytical HPLC and mass spectral analysis by SynBioSci Corporation (Livermore, CA), which showed that all of the peptides were ≥98% pure.…”

Section: Introductionmentioning

confidence: 99%

Determination of the Adsorption Free Energy for Peptide−Surface Interactions by SPR Spectroscopy

2008

View full text Add to dashboard Cite

To understand and predict protein adsorption behavior, we must first understand the fundamental interactions between the functional groups presented by the amino acid residues making up a protein and the functional groups presented by the surface. Limited quantitative information is available, however, on these types of submolecular interactions. The objective of this study was therefore to develop a reliable method to determine the standard state adsorption free energy (ΔG°a ds ) of amino acid residue-surface interactions using surface plasma resonance (SPR) spectroscopy. Two problems are commonly encountered when using SPR for peptide adsorption studies: the need to account for "bulk-shift" effects and the influence of peptide-peptide interactions at the surface. Bulk-shift effects represent the contribution of the bulk solute concentration to the SPR response that occurs in addition to the response due to adsorption. Peptide-peptide interactions, which are assumed to be zero for Langmuir adsorption, can greatly skew the isotherm shape and result in erroneous calculated values of ΔG°a ds . To address these issues, we have developed a new approach for the determination of ΔG°a ds using SPR that is based on the chemical potential. In this article, we present the development of this new approach and its application for the calculation of ΔG°a ds for a set of peptide-surface systems where the peptide has a host-guest amino acid sequence of TGTG-X-GTGT (where G and T are glycine and threonine residues and X represents a variable residue) and the surface consists of alkanethiol self-assembled monolayers (SAMs) with methyl (CH 3 ) and hydroxyl (OH) functionality. This new approach enables bulk-shift effects to be directly determined from the raw SPR versus peptide concentration data plots and the influence of peptide-peptide interaction effects to be minimized, thus providing a very straightforward and accurate method for the determination of ΔG °a ds for peptide adsorption. Further studies are underway to characterize ΔG°a ds for a large library of peptide-SAM combinations.

show abstract

Untitled

Cited by 4 publications

References 10 publications

Increased stability of human growth hormone with reduced lactogenic potency

Increased stability of human growth hormone with reduced lactogenic potency

Immobilized metal-ion affinity systems for recovery and structure–function studies of proteins at molecular, supramolecular, and cellular levels

Determination of the Adsorption Free Energy for Peptide−Surface Interactions by SPR Spectroscopy

Contact Info

Product

Resources

About