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Trends in the Design and Development of Specific Aptamers Against Peptides and Proteins.

Authors :
Tabarzad, Maryam
Jafari, Marzieh
Source :
Protein Journal. Apr2016, Vol. 35 Issue 2, p81-99. 19p.
Publication Year :
2016

Abstract

Aptamers are single stranded oligonucleotides, comparable to monoclonal antibodies (mAbs) in selectivity and affinity and have significant strategic properties in design, development and applications more than mAbs. Ease of design and development, simple chemical modification and the attachment of functional groups, easily handling and more adaptability with analytical methods, small size and adaptation with nanostructures are the valuable characteristics of aptamers in comparison to large protein based ligands. Among a broad range of targets that their specific aptamers developed, proteins and peptides have significant position according to the number of related studies performed so far. Since proteins control many of important physiological and pathological incidents in the living organisms, particularly human beings and because of the benefits of aptamers in clinical and analytical applications, aptamer related technologies in the field of proteins and peptides are under progress, exclusively. Currently, there is only one FDA approved therapeutic aptamer in the pharmaceutical market, which is specific to vascular endothelial growth factor and is prescribed for age related macular degenerative disease. Additionally, there are several aptamers in the different phases of clinical trials. Almost all of these aptamers are specific to clinically important peptide or protein targets. In addition, the application of protein specific aptamers in the design and development of targeted drug delivery systems and diagnostic biosensors is another intersting field of aptamer technology. In this review, significant efforts related to development and applications of aptamer technologies in proteins and peptides sciences were considered to emphasis on the importance of aptamers in medicinal and clinical applications. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
15723887
Volume :
35
Issue :
2
Database :
Academic Search Index
Journal :
Protein Journal
Publication Type :
Academic Journal
Accession number :
114188966
Full Text :
https://doi.org/10.1007/s10930-016-9653-2