Nothing Special   »   [go: up one dir, main page]

Ostresh et al., 2017 - Google Patents

Reversed-phase chromatography: the effect of induced conformations on peptide retention

Ostresh et al., 2017

Document ID
16373897925045268525
Author
Ostresh J
Büttner K
Houghten R
Publication year
Publication venue
High-Performance Liquid Chromatography of Peptides and Proteins

External Links

Snippet

Reversed-phase high-performance liquid chromatography (RPC) is the method of choice for the rapid estimation of the homogeneity of synthetic peptides. The possibility of using RPC" retention coefficients" for the prediction of peptide retention times is based generally upon …
Continue reading at www.taylorfrancis.com (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K7/00Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
    • C07K7/04Linear peptides containing only normal peptide links
    • C07K7/08Linear peptides containing only normal peptide links having 12 to 20 amino acids
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K1/00General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
    • C07K1/14Extraction; Separation; Purification
    • C07K1/16Extraction; Separation; Purification by chromatography
    • C07K1/22Affinity chromatography or related techniques based upon selective absorption processes
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K7/00Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
    • C07K7/04Linear peptides containing only normal peptide links
    • C07K7/06Linear peptides containing only normal peptide links having 5 to 11 amino acids
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/52Cytokines; Lymphokines; Interferons
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/775Apolipopeptides
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K16/00Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/18Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K7/00Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
    • C07K7/64Cyclic peptides containing only normal peptide links
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K16/00Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/12Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
    • C07K16/1203Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria
    • C07K16/1228Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
    • C07K16/1232Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia from Escherichia (G)
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids

Similar Documents

Publication Publication Date Title
Mant et al. Mixed‐mode hydrophilic interaction/cation‐exchange chromatography (HILIC/CEX) of peptides and proteins
Kovacs et al. Determination of intrinsic hydrophilicity/hydrophobicity of amino acid side chains in peptides in the absence of nearest‐neighbor or conformational effects
Guo et al. Prediction of peptide retention times in reversed-phase high-performance liquid chromatography I. Determination of retention coefficients of amino acid residues of model synthetic peptides
Sikora et al. The role of counter-ions in peptides—an overview
JP5873016B2 (en) Protein purification method using amino acids
Koga et al. Isolation and characterization of subunit polypeptides from apoproteins of rat serum lipoprotein
BR112012002934B1 (en) CHROMATOGRAPHIC PROCESSES AND THEIR PURIFIED COMPOUNDS
Wang et al. New tetrapeptide ligands designed for antibody purification with biomimetic chromatography: Molecular simulation and experimental validation
Mant et al. [19] Analysis of synthetic peptides by high-performance liquid chromatography
Simon et al. Conformational energy calculations of the effects of sequence variations on the conformations of two tetrapeptides
Young et al. Immunochemical studies on tobacco mosaic virus protein. V. The solid-phase synthesis of peptides of an antigenically active decapeptide of tobacco mosaic virus protein and the reaction of these peptides with antibodies to the whole protein
Hartmann et al. Comparison of reversed-phase liquid chromatography and hydrophilic interaction/cation-exchange chromatography for the separation of amphipathic α-helical peptides with L-and D-amino acid substitutions in the hydrophilic face
Ostresh et al. Reversed-phase chromatography: the effect of induced conformations on peptide retention
Hodges et al. Monitoring the hydrophilicity/hydrophobicity of amino acid side-chains in the non-polar and polar faces of amphipathic α-helices by reversed-phase and hydrophilic interaction/cation-exchange chromatography
Hearn et al. Determination of Biophysical Parameters of Polypeptide Retro− Inverso Isomers and Their Analogues by Capillary Electrophoresis
Bluard-Deconinck et al. Amino acid sequence of cysteic peptides of lactoferrin and demonstration of similarities between lactoferrin and transferrin
Mant et al. An improved approach to hydrophilic interaction chromatography of peptides: Salt gradients in the presence of high isocratic acetonitrile concentrations
KR20220082001A (en) Method for quantification of amino group-containing compounds protected by a protecting group having an Fmoc backbone
US20170146547A1 (en) Rp-hplc analysis of complex polypeptide mixtures
Chen et al. Selectivity differences in the separation of amphipathic α-helical peptides during reversed-phase liquid chromatography at pHs 2.0 and 7.0: effects of different packings, mobile phase conditions and temperature
Kirby et al. Separation of neuropeptide Y diastereomers by high-performance liquid chromatography and capillary zone electrophoresis
Popa et al. Capillary zone electrophoresis of α-helical diastereomeric peptide pairs with anionic ion-pairing reagents
Pen et al. Structural comparison of two esterases from Drosophila mojavensis isolated by immunoaffinity chromatography
Doughty et al. The contribution of helical potential to the in vitro receptor binding activity of a neuropeptide YN‐terminal deletion fragment
Kovacs et al. Quantitation of the nearest-neighbour effects of amino acid side-chains that restrict conformational freedom of the polypeptide chain using reversed-phase liquid chromatography of synthetic model peptides with L-and D-amino acid substitutions