Introduction
The protocols for the experiments resulting in each of the
measurements reported here is available on the experiments
page, to allow for replication or adaptation by other iGEM teams. We
also cite relevant sources for our protocols here. For data
availability, see the results page.
PFOA Aptamer
PFOA_JYP_21
Flurophore-Quencher Affinity
Assay
- Measurement: Binding Affinity (KD) of
PFOA_JYP_2 to its target PFOA, more details on experiments
page
- Novelty: Replication of Park, J et al.1
- Agreement: moderate discrepancy ( ≈ 2 orders of magnitude)
- Originally reported: 5.5 ⋅ 10−6M
- Our measurement: 2 ⋅ 10−4M
- Controls:
- This was a pilot experiment. It is possible that with more
controlled conditions (performing everything within the plate reader,
not having to move reagents between labs mid-experiment) we could have
gotten closer to the originally reported value. However, the conditions
were still generally controlled for.
- Usefulness:
- Other iGEM teams and researchers may want to consider
double-checking the KD of the
aptamer before commiting to it if they are considering using it, because
of the moderate discrepancy in binding affinity which, if correct, may
be application critical. However, as our experiment was a pilot this is
in no way intended to serve as a high-confidence challenge.
- Our replication does validate that aptamer system does qualitatively
bind to PFOA, despite the quantitative discrepancy on binding
affinity
Progesterone Aptamer
P4G032
A literature search did not reveal any papers mentioning the
P4G03 aptamer for progesterone following the paper that
originally reported it2, so to our
knowledge all results we present that are not replications of Jiménez,
G. C. et al. represent novel measurements. The Jiménez, G. C. et
al. paper focused most attention to the P4G13 aptamer as
they measured it with a greater conformational change when exposed to
progesterone, but the P4G03 aptamer had a lower KD value.
Isothermal
Titration Calorimetry (ITC) Experiment
- Measurement: Binding Affinity (KD) of
P4G03 sequence to its target progesterone (with no
modifications)
- Novelty: novel measurement method, same value reported in Jiménez,
G. C. et al.
- Although KD values were
reported for
P4G03 in the original paper2, these values were only calculated for
P4G03 using fluoresence, so our use of ITC represents a
novel method for calcuclating this value.
- Agreement: minor discrepancy ( < 1 order of magnitude)
- Originally reported value (fluoresence): 9.63 ± 3.12 nM
- Our measurement (ITC): 50 nM
- Controls:
- The controls that needed to be run to calculate this KD are buffer
only into buffer only showing zero heat changes. Another control of
target molecule diluted in buffer into buffer only must be subtracted
from experimental run of target molecule diluted in buffer into aptamer
diluted in buffer. These were all controls that we fulfilled to
correctly calculate the KD. The specific
protocol we followed with the concentrations used for our buffers and
our experimental conditions is on our experiments
page.
- Usefulness:
- Other iGEM teams and researchers have a novel validation that
P4G03 binds progesterone with binding affinity within the
tens-of-nanomolar range
- this value can be used for calculations and for initial analysis to
see if this aptamer is a good fit for the chosen application
- This may serve as a green light for teams that are looking for a
very sensitive aptamer for progesterone
- the slight discrepancy may be related to differences of measurement
methods
- This measurement does not assess any potential electrochemical
modifications of the
P4G03 sequence
Circular Dichroism (CD)
Experiments
- Measurement: Qualitative determination, “Does the aptamer display
significant conformational change given changing values of target?”
- qualitative measurement
- inferred from quantitative data through visualizations
- Novelty:
P4G03 with intended target (progesterone): replication
with modifications
- original experiment reported in Jiménez, G. C. et al. supplementary
information used only two concentrations, where no progesterone and
1μM aptamer were
compared with 1μM of
both progesterone and aptamer.
- In contrast, our experimental concentrations were higher, with
starting concentrations of progesterone at 100μM * (108/280) ≈ 39μM.
- We tested multiple ratios of progesterone to aptamer.
P4G03 with DHT, P4G03 with cholesterol:
novel, and no analagous experiments for P4G13 reported in
Jiménez, G. C. et al.
- Cross reactivity experiments in Jiménez, G. C. et al. were focused
on making sure
P4G13 is specific to progesterone against
environmentally relevant hormones. No cross-reactivity experiments were
performed for the distinct P4G03 aptamer, which was not
selected for further study due to lower conformational change, despite
its higher KD.
- Additionally, no experiments were reported by Jiménez, G. C. et
al. investigating the clinically relevant hormones DHT and cholesterol,
as the cross-reactivity experiments were focused on environmental
applications
- Agreement:
- Our CD experiments with
P4G03 appear to display greater
response conformational change than those in Jiménez, G. C. et al.,
which may just be due to the increased concentrations and more extreme
ratios of aptamer and progesterone that we used.
- Controls:
- Aptamer only (to establish the baseline CD signature)
- Ligand only (progesterone, DHT, cholesterol)
- Buffer only
- Ethanol-only solvent control (confirming ethanol concentration did
not affect the CD signal)
- Equal steroid hormone ratios: All ligands tested at identical molar
ratios (0.2:1, 5:1, 20:1 in our last experiment) and solvent
compositions.
- The CD spectrometer was zeroed with a clean ethanol/PBS buffer
baseline before each scan. Temperature stability was confirmed at 37 °C
throughout. No instrumental drift was detected.
- Usefulness:
- We were able to confirm some conformational change of
P4G03, however the relative magnitude compared with that
reported in Jiménez, G. C. et al. is ambiguous due to different test
concentrations. Our data may be useful for future analysis to better
characterize the conformational change of P4G03 across a
wider variety of concentrations.
- We validated that the
P4G03 is specific to progesterone
against two important clinical cross-reactants, eliminating potential
concerns about this aptamer for future iGEM teams who may desire to use
it for health applications.
Alternating
Current (AC) Voltammetry Experiments
- Measurement: the impedimetric response of the electrochemically
modified P4G03 aptamer to progesterone in solution
- essentially changes in a current/voltage graph due to changing
solution concentrations of target (progesterone)
- Novelty: Novel. Similar electrochemical experiments were conducted
by Jiménez, G. C. et al. for
P4G13 and P4G11
aptamers.
- Controls:
- Our data still needs to be improved - we need to have better
controls particularly in running the experiment without progesterone
compared running it with progesterone over time to determine a change in
voltage to eliminate the change of voltage in the instrument to
determine if these measurements our useful. That is our top priority at
the moment is to improve our controls on this experiment, so that this
data can be used to create a baseline of the voltage of an aptamer
sensor without any progesterone bound compared to having progesterone
bound.
- Usefulness:
- we have witnessed some signal from this aptamer, so our qualitative
measurement that this aptamer does respond through bio-impedance to
progesterone should signal to future iGEM teams that this aptamer may be
worth considering for their purposes.
References
Park, J., Yang, K.-A., Choi, Y. & Choe, J. K. Novel ssDNA
aptamer-based fluorescence sensor for perfluorooctanoic acid detection
in water. Environ. Int. 158, 107000 (2022).
Jiménez, G. C. et al. Aptamer-Based Label-Free Impedimetric
Biosensor for Detection of Progesterone. ACS Publications
https://pubs.acs.org/doi/pdf/10.1021/ac503639s (2015)
doi:10.1021/ac503639s.