Affiliate Associate Professor of Biochemistry, Biophysics and Molecular Biology
My laboratory seeks to describe how immune system activation is tuned by carbohydrate chains (glycans) attached to
proteins. This research direction seeks to identify novel disease therapies by studying the effect of molecular structure
perturbations on immune cell responses. Our primary target is immunoglobulin G (IgG), a circulatory protein expressed
to recognize foreign particles and initiate an immune response by activating Fcg Receptors. The structure of a glycan
attached to Asn297 of the IgG Fragment crystallizable (Fc) domain influences the strength of the body’s response. Certain forms of this glycan are particularly prevalent in patients with autoimmune disorders, notably rheumatoid arthritis,
though it is unclear why. These same glycan forms also perturb the Fc – Fcg Receptor interaction, though a biophysical mechanism linking the Fc glycan and immune activation has not yet been described. We use a wide variety of techniques, including: solution nuclear magnetic resonance spectroscopy, mass spectrometry, enzyme assays, mammalian and
bacterial protein expression, as well as cell-based assays of macrophage and natural killer cell activation. We are also interested in designing enzymes to accept non-native substrates. Enzymes of the polyketide synthesis
machinery are being explored for their ability to accept substrate analogs with added chemical functionality. This effort is
funded by the Center for BioRenewable Chemicals (www.cbirc.iastate.edu).
read more
proteins. This research direction seeks to identify novel disease therapies by studying the effect of molecular structure
perturbations on immune cell responses. Our primary target is immunoglobulin G (IgG), a circulatory protein expressed
to recognize foreign particles and initiate an immune response by activating Fcg Receptors. The structure of a glycan
attached to Asn297 of the IgG Fragment crystallizable (Fc) domain influences the strength of the body’s response. Certain forms of this glycan are particularly prevalent in patients with autoimmune disorders, notably rheumatoid arthritis,
though it is unclear why. These same glycan forms also perturb the Fc – Fcg Receptor interaction, though a biophysical mechanism linking the Fc glycan and immune activation has not yet been described. We use a wide variety of techniques, including: solution nuclear magnetic resonance spectroscopy, mass spectrometry, enzyme assays, mammalian and
bacterial protein expression, as well as cell-based assays of macrophage and natural killer cell activation. We are also interested in designing enzymes to accept non-native substrates. Enzymes of the polyketide synthesis
machinery are being explored for their ability to accept substrate analogs with added chemical functionality. This effort is
funded by the Center for BioRenewable Chemicals (www.cbirc.iastate.edu).
×
About Adam Barb
My laboratory seeks to describe how immune system activation is tuned by carbohydrate chains (glycans) attached to
proteins. This research direction seeks to identify novel disease therapies by studying the effect of molecular structure
perturbations on immune cell responses. Our primary target is immunoglobulin G (IgG), a circulatory protein expressed
to recognize foreign particles and initiate an immune response by activating Fcg Receptors. The structure of a glycan
attached to Asn297 of the IgG Fragment crystallizable (Fc) domain influences the strength of the body’s response. Certain forms of this glycan are particularly prevalent in patients with autoimmune disorders, notably rheumatoid arthritis,
though it is unclear why. These same glycan forms also perturb the Fc – Fcg Receptor interaction, though a biophysical mechanism linking the Fc glycan and immune activation has not yet been described. We use a wide variety of techniques, including: solution nuclear magnetic resonance spectroscopy, mass spectrometry, enzyme assays, mammalian and
bacterial protein expression, as well as cell-based assays of macrophage and natural killer cell activation. We are also interested in designing enzymes to accept non-native substrates. Enzymes of the polyketide synthesis
machinery are being explored for their ability to accept substrate analogs with added chemical functionality. This effort is
funded by the Center for BioRenewable Chemicals (www.cbirc.iastate.edu).
proteins. This research direction seeks to identify novel disease therapies by studying the effect of molecular structure
perturbations on immune cell responses. Our primary target is immunoglobulin G (IgG), a circulatory protein expressed
to recognize foreign particles and initiate an immune response by activating Fcg Receptors. The structure of a glycan
attached to Asn297 of the IgG Fragment crystallizable (Fc) domain influences the strength of the body’s response. Certain forms of this glycan are particularly prevalent in patients with autoimmune disorders, notably rheumatoid arthritis,
though it is unclear why. These same glycan forms also perturb the Fc – Fcg Receptor interaction, though a biophysical mechanism linking the Fc glycan and immune activation has not yet been described. We use a wide variety of techniques, including: solution nuclear magnetic resonance spectroscopy, mass spectrometry, enzyme assays, mammalian and
bacterial protein expression, as well as cell-based assays of macrophage and natural killer cell activation. We are also interested in designing enzymes to accept non-native substrates. Enzymes of the polyketide synthesis
machinery are being explored for their ability to accept substrate analogs with added chemical functionality. This effort is
funded by the Center for BioRenewable Chemicals (www.cbirc.iastate.edu).
| Present | Assistant Professor, Iowa State University ‐ Department of Biochemistry, Biophysics and Molecular Biology | |
|
|
||
Disciplines
Research Interests
Courses
- BBMB 102 Introduction Biochemistry
- BBMB 552 Nuclear Magnetic Resonance
- BBMB 622 Graduate Carbohydrate Chemistry
Contact Information
4210 Molecular Bio
2437 Pammel Dr
Ames, IA 50011-1079
Phone: 515-294-8928
Fax: 515-294-7629
Email: