Overview
I graduated from the University of Exeter in June 2015 with a bachelor’s degree in Biological and Medicinal Chemistry. My past research has involved protein characterisation and the development of synthetic biology as a tool to combat explosive waste pollution.
Currently my research is focused on biomarker screening to provide rapid diagnosis of infection and insightful antibiotic selection. In September 2015 I began my EPSRC funded PhD in biotechnology, under the supervision of Dr Chris Hyde and Professor Andrew Shaw.
Qualifications
BSc Biological and Medicinal Chemistry
Research
Research interests
My PhD project is based on the development and application of a novel biophotonic array sensor, designed for observing specific antibody / antigen interactions. I am predominantly interested in a subset of blood plasma proteins known as the Complement cascade.
Rapid quantification of Complement proteins in patient blood could provide an early warning of infection, the nature of the causative organism and even identify individuals predisposed to higher risk of post-operative complications.
Publications
Key publications | Publications by category | Publications by year
Publications by category
Journal articles
Reader P, Shaw A, Hyde C, Olkhov R (2019). A rapid and quantitative technique for assessing IgG monomeric purity, calibrated with the NISTmAb reference material.
Analytical and Bioanalytical Chemistry Full text.
Reader PP, Shaw AM (2017). Kinetic Analysis of the Multivalent Ligand Binding Interaction between Protein A/G and IgG: a Standard System Setting.
Journal of Physical Chemistry B,
121(38), 8919-8925.
Abstract:
Kinetic Analysis of the Multivalent Ligand Binding Interaction between Protein A/G and IgG: a Standard System Setting
© 2017 American Chemical Society. Recombinant protein A/G (PAG) has a sequence coding for eight IgG binding sites and has enhanced interspecies affinity. High-frequency sampling of a PAG titration with IgG produces concentration profiles that are sensitive to the kinetic availability of the binding sites. The full kinetic model developed here for IgG binding sequentially to PAG shows only two distinct kinetic processes, describing an initial rapid association of two antibodies to PAG with a rate constant k-fast = (1.86 ± 0.08) × 106 M-1 s-1 and a slower antibody binding process to all remaining sites, k-slow = (1.24 ± 0.05) × 104 M-1 s-1. At equilibrium (after 1 h), the maximum IgG occupancy of PAG is 2.8 ± 0.5, conflicting with the genetic evidence of eight binding sites and suggesting significant steric hindrance of the neighboring IgG binding sites. The phosphate-buffered saline (PBS) solution defines a standard system setting, and this may be compared with other settings. The mean association rate of PAG-IgGn in the standard setting is 282 ± 20% higher than when PAG is tethered to a surface. A systems biology approach requires that a model parameter set that defines a system in a standard setting should be transferable to another system. The transfer of parameters between settings may be performed using activity coefficients characterizing an effective concentration of species in a system, ai = γici. The activity correction, γ, for the eight-site occupancy is γ = 0.35 ± 0.06, and mapping from the standard setting to the solution setting suggests γPAG-IgG = 0.4 ± 0.03. The role of activity coefficients and transferability of kinetic parameters between system settings is discussed. (Graph Presented).
Abstract.
Full text.
Publications by year
2019
Reader P, Shaw A, Hyde C, Olkhov R (2019). A rapid and quantitative technique for assessing IgG monomeric purity, calibrated with the NISTmAb reference material.
Analytical and Bioanalytical Chemistry Full text.
2017
Reader PP, Shaw AM (2017). Kinetic Analysis of the Multivalent Ligand Binding Interaction between Protein A/G and IgG: a Standard System Setting.
Journal of Physical Chemistry B,
121(38), 8919-8925.
Abstract:
Kinetic Analysis of the Multivalent Ligand Binding Interaction between Protein A/G and IgG: a Standard System Setting
© 2017 American Chemical Society. Recombinant protein A/G (PAG) has a sequence coding for eight IgG binding sites and has enhanced interspecies affinity. High-frequency sampling of a PAG titration with IgG produces concentration profiles that are sensitive to the kinetic availability of the binding sites. The full kinetic model developed here for IgG binding sequentially to PAG shows only two distinct kinetic processes, describing an initial rapid association of two antibodies to PAG with a rate constant k-fast = (1.86 ± 0.08) × 106 M-1 s-1 and a slower antibody binding process to all remaining sites, k-slow = (1.24 ± 0.05) × 104 M-1 s-1. At equilibrium (after 1 h), the maximum IgG occupancy of PAG is 2.8 ± 0.5, conflicting with the genetic evidence of eight binding sites and suggesting significant steric hindrance of the neighboring IgG binding sites. The phosphate-buffered saline (PBS) solution defines a standard system setting, and this may be compared with other settings. The mean association rate of PAG-IgGn in the standard setting is 282 ± 20% higher than when PAG is tethered to a surface. A systems biology approach requires that a model parameter set that defines a system in a standard setting should be transferable to another system. The transfer of parameters between settings may be performed using activity coefficients characterizing an effective concentration of species in a system, ai = γici. The activity correction, γ, for the eight-site occupancy is γ = 0.35 ± 0.06, and mapping from the standard setting to the solution setting suggests γPAG-IgG = 0.4 ± 0.03. The role of activity coefficients and transferability of kinetic parameters between system settings is discussed. (Graph Presented).
Abstract.
Full text.
Peter_Reader Details from cache as at 2019-08-21 18:08:16
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External Engagement and Impact
Awards
2015 | College Commendation for Academic Excellence
Editorial responsibilities
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