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Counteracting roles of AMP deaminase and AMP kinase in the development of fatty liver

PloS one, 2012-11, Vol.7 (11), p.e48801-e48801

2012

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Role of Peptide Hydrophobicity in the Mechanism of Action of α-Helical Antimicrobial Peptides

Antimicrobial Agents and Chemotherapy, 2007-04, Vol.51 (4), p.1398-1406

2007

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Opposing activity changes in AMP deaminase and AMP-activated protein kinase in the hibernating ground squirrel

PloS one, 2015-04, Vol.10 (4), p.e0123509-e0123509

2015

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Mixed-mode hydrophilic interaction/cation-exchange chromatography (HILIC/CEX) of peptides and proteins

Journal of separation science, 2008-08, Vol.31 (15), p.2754-2773

2008

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Determination of intrinsic hydrophilicity/hydrophobicity of amino acid side chains in peptides in the absence of nearest-neighbor or conformational effects

Biopolymers, 2006, Vol.84 (3), p.283-297

2006

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Mixed-mode hydrophilic interaction/cation-exchange chromatography: Separation of complex mixtures of peptides of varying charge and hydrophobicity

Journal of separation science, 2008-05, Vol.31 (9), p.1573-1584

2008

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Purification and structural characterization of siderophore (corynebactin) from Corynebacterium diphtheriae

PloS one, 2012-04, Vol.7 (4), p.e34591-e34591

2012

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De Novo Designed Amphipathic α‑Helical Antimicrobial Peptides Incorporating Dab and Dap Residues on the Polar Face To Treat the Gram-Negative Pathogen, Acinetobacter baumannii

Journal of medicinal chemistry, 2019-04, Vol.62 (7), p.3354-3366

2019

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Reversed-phase HPLC of peptides: Assessing column and solvent selectivity on standard, polar-embedded and polar endcapped columns

Journal of separation science, 2010-10, Vol.33 (19), p.3005-3021

2010

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Role of positively charged residues on the polar and non‐polar faces of amphipathic α‐helical antimicrobial peptides on specificity and selectivity for Gram‐negative pathogens

Chemical biology & drug design, 2018-01, Vol.91 (1), p.75-92

2018

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Separation of highly charged (+5 to +10) amphipathic α-helical peptide standards by cation-exchange and reversed-phase high-performance liquid chromatography

Journal of Chromatography A, 2018-11, Vol.1574, p.60-70

2018

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Rational Design of α-Helical Antimicrobial Peptides with Enhanced Activities and Specificity/Therapeutic Index

The Journal of biological chemistry, 2005-04, Vol.280 (13), p.12316-12329

2005

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Optimized purification of a fusion protein by reversed-phase high performance liquid chromatography informed by the linear solvent strength model

Journal of Chromatography A, 2017-10, Vol.1521, p.44-52

2017

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Structure–activity relationships of the antimicrobial peptide gramicidin S and its analogs: Aqueous solubility, self-association, conformation, antimicrobial activity and interaction with model lipid membranes

Biochimica et biophysica acta, 2014-05, Vol.1838 (5), p.1420-1429

2014

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Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: Comparison with other hydrophilicity/hydrophobicity scales

Biopolymers, 2009, Vol.92 (6), p.573-595

2009

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Design of peptide standards with the same composition and minimal sequence variation to monitor performance/selectivity of reversed-phase matrices

Journal of Chromatography A, 2012-03, Vol.1230, p.30-40

2012

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Platform technology to generate broadly cross-reactive antibodies to α-helical epitopes in hemagglutinin proteins from influenza A viruses

Biopolymers, 2016-03, Vol.106 (2), p.144-159

2016

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An improved approach to hydrophilic interaction chromatography of peptides: Salt gradients in the presence of high isocratic acetonitrile concentrations

Journal of Chromatography A, 2013-02, Vol.1277, p.15-25

2013

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Preparative reversed-phase high-performance liquid chromatography collection efficiency for an antimicrobial peptide on columns of varying diameters (1 mm to 9.4 mm I.D.)

Journal of Chromatography A, 2007-01, Vol.1140 (1), p.112-120

2007

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Separation of Peptides on HALO 2‐Micron Particles

Current Protocols in Protein Science, 2016-08, Vol.85 (1), p.11.6.1-11.6.16

2016

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Requirements for prediction of peptide retention time in reversed-phase high-performance liquid chromatography: Hydrophilicity/hydrophobicity of side-chains at the N- and C-termini of peptides are dramatically affected by the end-groups and location

Journal of Chromatography A, 2007-02, Vol.1141 (2), p.212-225

2007

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Effects of Hydrophobicity on the Antifungal Activity of α-Helical Antimicrobial Peptides

Chemical biology & drug design, 2008-12, Vol.72 (6), p.483-495

2008

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Structure-guided RP-HPLC chromatography of diastereomeric α-helical peptide analogs substituted with single amino acid stereoisomers

Biomedical chromatography, 2014-04, Vol.28 (4), p.511-517

2014

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HPLC analysis and purification of peptides

Methods in molecular biology (Clifton, N.J.), 2007, Vol.386, p.3

2007

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Comparison of Biophysical and Biologic Properties of α-Helical Enantiomeric Antimicrobial Peptides

Chemical biology & drug design, 2006-02, Vol.67 (2), p.162-173

2006

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Counteracting roles of AMP deaminase and AMP kinase in the development of fatty liver

Role of Peptide Hydrophobicity in the Mechanism of Action of α-Helical Antimicrobial Peptides

Opposing activity changes in AMP deaminase and AMP-activated protein kinase in the hibernating ground squirrel

Mixed-mode hydrophilic interaction/cation-exchange chromatography (HILIC/CEX) of peptides and proteins

Determination of intrinsic hydrophilicity/hydrophobicity of amino acid side chains in peptides in the absence of nearest-neighbor or conformational effects

Mixed-mode hydrophilic interaction/cation-exchange chromatography: Separation of complex mixtures of peptides of varying charge and hydrophobicity

Purification and structural characterization of siderophore (corynebactin) from Corynebacterium diphtheriae

De Novo Designed Amphipathic α‑Helical Antimicrobial Peptides Incorporating Dab and Dap Residues on the Polar Face To Treat the Gram-Negative Pathogen, Acinetobacter baumannii

Reversed-phase HPLC of peptides: Assessing column and solvent selectivity on standard, polar-embedded and polar endcapped columns

Role of positively charged residues on the polar and non‐polar faces of amphipathic α‐helical antimicrobial peptides on specificity and selectivity for Gram‐negative pathogens

Separation of highly charged (+5 to +10) amphipathic α-helical peptide standards by cation-exchange and reversed-phase high-performance liquid chromatography

Rational Design of α-Helical Antimicrobial Peptides with Enhanced Activities and Specificity/Therapeutic Index

Optimized purification of a fusion protein by reversed-phase high performance liquid chromatography informed by the linear solvent strength model

Structure–activity relationships of the antimicrobial peptide gramicidin S and its analogs: Aqueous solubility, self-association, conformation, antimicrobial activity and interaction with model lipid membranes

Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: Comparison with other hydrophilicity/hydrophobicity scales

Design of peptide standards with the same composition and minimal sequence variation to monitor performance/selectivity of reversed-phase matrices

Platform technology to generate broadly cross-reactive antibodies to α-helical epitopes in hemagglutinin proteins from influenza A viruses

An improved approach to hydrophilic interaction chromatography of peptides: Salt gradients in the presence of high isocratic acetonitrile concentrations

Preparative reversed-phase high-performance liquid chromatography collection efficiency for an antimicrobial peptide on columns of varying diameters (1 mm to 9.4 mm I.D.)

Separation of Peptides on HALO 2‐Micron Particles

Requirements for prediction of peptide retention time in reversed-phase high-performance liquid chromatography: Hydrophilicity/hydrophobicity of side-chains at the N- and C-termini of peptides are dramatically affected by the end-groups and location

Effects of Hydrophobicity on the Antifungal Activity of α-Helical Antimicrobial Peptides

Structure-guided RP-HPLC chromatography of diastereomeric α-helical peptide analogs substituted with single amino acid stereoisomers

HPLC analysis and purification of peptides

Comparison of Biophysical and Biologic Properties of α-Helical Enantiomeric Antimicrobial Peptides

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