2023
DOI: 10.1016/j.cjac.2022.100219
|View full text |Cite
|
Sign up to set email alerts
|

Serum stability of 5 cholesterol triethylene glycol-26-OKA and 39 cholesterol triethylene glycol-24-OKA modified protoporphyrin IX DNA-aptamer and their in vitro heme binding characteristics

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
2

Citation Types

0
2
2

Year Published

2023
2023
2023
2023

Publication Types

Select...
2

Relationship

1
1

Authors

Journals

citations
Cited by 2 publications
(5 citation statements)
references
References 27 publications
0
2
2
Order By: Relevance
“…It can be extracted from this experiment that conjugation of cholesterol triethylene glycol to OKA_24 ( = 27.62 ± 1.2 nM) and OKA_26 ( = 15.2 ± 1.68 nM) leads to decrease in binding affinity for heme by 3-fold in both COL-TEG_26-OKA ( = 4 7.13 ± 3.767 nM) and COL-TEG_24-OKA ( = 84.6 ± 8.7 nM) conjugate. Despite the fact that these findings disagreed with the prior findings obtained by carrying out an ultraviolet visible spectrum titrations of native and lipid conjugated aptamers with heme, [5] , it is not surprising because of the role played by the environmental influence on the conformation of molecules which can either enhance or reduce their activity [20] , [21] . Immobilization of heme on a glutaraldehyde-cysteamine coated gold electrode, for example, improved the binding affinity of both modified and unmodified aptamers for heme relative to their respective binding affinity in buffer solutions analyzed by UV spectral titration [5] (data not shown).…”
Section: Resultscontrasting
confidence: 86%
See 3 more Smart Citations
“…It can be extracted from this experiment that conjugation of cholesterol triethylene glycol to OKA_24 ( = 27.62 ± 1.2 nM) and OKA_26 ( = 15.2 ± 1.68 nM) leads to decrease in binding affinity for heme by 3-fold in both COL-TEG_26-OKA ( = 4 7.13 ± 3.767 nM) and COL-TEG_24-OKA ( = 84.6 ± 8.7 nM) conjugate. Despite the fact that these findings disagreed with the prior findings obtained by carrying out an ultraviolet visible spectrum titrations of native and lipid conjugated aptamers with heme, [5] , it is not surprising because of the role played by the environmental influence on the conformation of molecules which can either enhance or reduce their activity [20] , [21] . Immobilization of heme on a glutaraldehyde-cysteamine coated gold electrode, for example, improved the binding affinity of both modified and unmodified aptamers for heme relative to their respective binding affinity in buffer solutions analyzed by UV spectral titration [5] (data not shown).…”
Section: Resultscontrasting
confidence: 86%
“…Despite the fact that these findings disagreed with the prior findings obtained by carrying out an ultraviolet visible spectrum titrations of native and lipid conjugated aptamers with heme, [5] , it is not surprising because of the role played by the environmental influence on the conformation of molecules which can either enhance or reduce their activity [20] , [21] . Immobilization of heme on a glutaraldehyde-cysteamine coated gold electrode, for example, improved the binding affinity of both modified and unmodified aptamers for heme relative to their respective binding affinity in buffer solutions analyzed by UV spectral titration [5] (data not shown). However, this increase in binding favors unmodified aptamers with 3-fold increase compared to lipid conjugated once.…”
Section: Resultscontrasting
confidence: 86%
See 2 more Smart Citations
“…Scientific considerations include factors like charge, size, binding affinity, and ligand stability. In the case of antibodies, it is also crucial to consider their potential to trigger antibody-dependent cell-mediated cytotoxicity 32 , 33 . Aptamers have further been incorporated into the development of nanomaterials for drug delivery purposes within biological environments 34 - 37 .…”
Section: Introductionmentioning
confidence: 99%