Highly Specific Recognition of Guanosine Using Engineered Base‐Excised Aptamers. Issue 60 (24th September 2020)
- Record Type:
- Journal Article
- Title:
- Highly Specific Recognition of Guanosine Using Engineered Base‐Excised Aptamers. Issue 60 (24th September 2020)
- Main Title:
- Highly Specific Recognition of Guanosine Using Engineered Base‐Excised Aptamers
- Authors:
- Li, Yuqing
Liu, Juewen - Abstract:
- Abstract: Purines and their derivatives are highly important molecules in biology for nucleic acid synthesis, energy storage, and signaling. Although many DNA aptamers have been obtained for binding adenine derivatives such as adenosine, adenosine monophosphate, and adenosine triphosphate, success for the specific binding of guanosine has been limited. Instead of performing new aptamer selections, we report herein a base‐excision strategy to engineer existing aptamers to bind guanosine. Both a Na + ‐binding aptamer and the classical adenosine aptamer have been manipulated as base‐excising scaffolds. A total of seven guanosine aptamers were designed, of which the G16‐deleted Na + aptamer showed the highest bindng specificity and affinity for guanosine with an apparent dissociation constant of 0.78 mm . Single monophosphate difference in the target molecule was also recognizable. The generality of both the aptamer scaffold and excised site were systematically studied. Overall, this work provides a few guanosine binding aptamers by using a non‐SELEX method. It also provides deeper insights into the engineering of aptamers for molecular recognition. Abstract : Guanosine binding : Base excision endows existing aptamers with new molecular recognition functions. After excising a specific guanine nucleotide from a Na + ‐binding or classical adenosine aptamer, the resulting DNA strands can specifically recognize guanosine, but guanosine monophosphate (GMP) and triphosphate (GTP) areAbstract: Purines and their derivatives are highly important molecules in biology for nucleic acid synthesis, energy storage, and signaling. Although many DNA aptamers have been obtained for binding adenine derivatives such as adenosine, adenosine monophosphate, and adenosine triphosphate, success for the specific binding of guanosine has been limited. Instead of performing new aptamer selections, we report herein a base‐excision strategy to engineer existing aptamers to bind guanosine. Both a Na + ‐binding aptamer and the classical adenosine aptamer have been manipulated as base‐excising scaffolds. A total of seven guanosine aptamers were designed, of which the G16‐deleted Na + aptamer showed the highest bindng specificity and affinity for guanosine with an apparent dissociation constant of 0.78 mm . Single monophosphate difference in the target molecule was also recognizable. The generality of both the aptamer scaffold and excised site were systematically studied. Overall, this work provides a few guanosine binding aptamers by using a non‐SELEX method. It also provides deeper insights into the engineering of aptamers for molecular recognition. Abstract : Guanosine binding : Base excision endows existing aptamers with new molecular recognition functions. After excising a specific guanine nucleotide from a Na + ‐binding or classical adenosine aptamer, the resulting DNA strands can specifically recognize guanosine, but guanosine monophosphate (GMP) and triphosphate (GTP) are excluded . … (more)
- Is Part Of:
- Chemistry. Volume 26:Issue 60(2020)
- Journal:
- Chemistry
- Issue:
- Volume 26:Issue 60(2020)
- Issue Display:
- Volume 26, Issue 60 (2020)
- Year:
- 2020
- Volume:
- 26
- Issue:
- 60
- Issue Sort Value:
- 2020-0026-0060-0000
- Page Start:
- 13644
- Page End:
- 13651
- Publication Date:
- 2020-09-24
- Subjects:
- aptamers -- biosensors -- DNA structures -- fluorescence -- nucleobases
Chemistry -- Periodicals
540 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1521-3765 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/chem.202001835 ↗
- Languages:
- English
- ISSNs:
- 0947-6539
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3168.860500
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 14850.xml