MODEL ABSTRACTS

Practice-based:

Pharmacy clients’ attitudes to expanded pharmacist

prescribing and the role of agency theory on involved
stakeholders
Kreshnik Hoti, Jeffery Hughes and Bruce Sunderland
Curtin Health and Innovation Research Institute and School of
Pharmacy, Curtin University Perth,WA, Australia

Objective To examine the views of regular pharmacy clients on

pharmacist prescribing and employ agency theory in considering the
relationship between the stakeholders involved.
Methods Computer assisted telephone interviews were conducted
with 400 pharmacy clients recruited aroundAustralia. Potential
respondents were identified using a random number generation
function in Microsoft Excel. Data were analysed with SPSS version 17
using one-way analysis of variance, principal component analysis and
linear regression. The relationships between the main stakeholders
involved were explored using agency theory. Key findings A total of
1153 answered calls recruited 400 consenting pharmacy clients. Most
respondents (71%) trusted pharmacists adopting an expanded role in
prescribing, however the majority (66%) supported this only after a
diagnosis had been made by a doctor. Those who accepted
pharmacist diagnosing and prescribing preferred that this was limited
to pain management and antibiotics. Most respondents (64%)
considered that expanded pharmacist prescribing would improve their
access to prescription medicines, although those over 65 years of age
were less supportive than younger respondents. Factors which
contributed positively to clients’ perception of trust in an expanded
prescribing role for pharmacists were identified, and improved access
to medicines was found to be the strongest predictor (P < 0.0001).
Conclusion Most pharmacy clients trusted pharmacists adopting an
expanded prescribing role, but preferred that this was limited to
doctors performing the initial diagnosis. Agency theory would
conceptualize the introduction of pharmacist prescribers, as disrupting
the principal (patient) agent (doctor) relationship. Its introduction
would best be facilitated by careful change management.

1
Lab-based:

Enhanced Protein Delivery from Photopolymerized Hydrogels Using

a Pseudospecific Metal Chelating Ligand
Chien-Chi Lin1 and Andrew T. Metters 1,2,3
1
Department of Bioengineering, Clemson University, Clemson, South
Carolina 29634, USA.
2
Department of Chemical and Biomolecular Engineering, Clemson
University, 127 Earle Hall, Clemson, South Carolina 29634, USA.
3
To whom the correspondence should be addressed. (e-mail: metters
@clemson.edu)

Purpose This study was conducted to investigate the cause of

incomplete protein release from photopolymerized poly(ethylene
glycol) (PEG) hydrogels and verify the protein-protection mechanism
provided by iminodiacetic acid (IDA).
Methods The in vitro release of bovine serum albumin (BSA) from
PEG hydrogels prepared under different conditions was studied.
Photoinitiator and initial protein concentrations were varied as well as
the addition of IDA and metal ions. Protein immobilization within the
nondegradable networks via free-radical reaction was demonstrated
by gel electrophoresis.
Results Protein release efficiency was shown to be dependent on
photoinitiator and initial protein concentration. Gel electrophoresis
results revealed immobilization of protein to the polymer network and
further indicated the detrimental role of free radicals in lowering
protein-release efficiency. Adding IDA to the prepolymer solution
enhanced total protein release from the subsequently
photopolymerized network in a dose-dependent manner. The addition
of metal ions including Cu 2+, Zn2+, and Ni2+ further increased BSA
release efficiency. Agreement between the protein release data and
theoretical model predictions accounting for reversible protein–IDA
binding further validated the protection effect provided by IDA and
IDA-transition metal complexes.
Conclusions The protection effect described in this study offers a
novel strategy for increasing the delivery efficiencies of many
therapeutically valuable proteins.