Abstract

Aptamers are small and specific oligonucleotides [RNA or single-strand DNA (ssDNA)] with a high binding affinity against target protein. In vitro selection process of aptamer by selective evolution of ligands by exponential enrichment (SELEX) has been invented in 1990 by Larry Gold and Jack Szostak. SELEX is a random amplification of target protein with combined oligonucleotide libraries and selection of synthesized aptamer by magnetic beads, affinity chromatography, and capillary electrophoresis-based methods. According to their low molecular weight, non-immunogenic feature in vivo, low production cost, high thermal stability, increase in production potential, and ample of modification capacities, aptamers are becoming essential medical tools for diagnosis and treatment of diseases such as macular degeneration, hemophilia, heart disease, and various cancer types. The therapeutic potential of aptamers, with high binding affinity against carcinogenesis-associated growth factors, receptors, or proteins frequently overexpressed in specific cancers such as prostate, breast, colon, lung, leukemia, hepatocellular, and cervical carcinoma. The strategies for aptamer-based drugs in cancer therapy design/modify aptamers against cancer biomarkers, accelerate immunotherapy targeting immune system, and increase the drug delivery in cancer cells. In conclusion, aptamers are promising candidate drugs due to their antiproliferative effect on cancer cells and the drug delivery systems during cancer chemotherapy.

Highlights

  • Aptamer is derived from one Latin and one Greek word combinations: “aptus,” which means “fit,” and “meros” meaning “particle” [1]

  • selective evolution of ligands by exponential enrichment (SELEX) is a consecutive processes starting with binding of target with random sequence of oligonucleotide library, washing and elution of unbound oligonucleotides, amplification of 3D structure oligonucleotides against the target epitope via polymerase chain reaction (PCR), selection of aptamers with high binding affinity and specificity, and modifications of novel aptamers to increase stability and function [3]

  • Since SELEX method is composed of generation of aptamer against target molecule by using a rich random nucleotide sequence of oligonucleotide libraries, there are modifications on SELEX method according to research aim such as nitrocellulose membrane filtration-based SELEX, affinity chromatography and magnetic bead-based SELEX, capillary electrophoresis-based SELEX, microfluidic-based SELEX, cell SELEX, and others [electromobility shift assay (EMSA), surface plasmon resonance (SPR)]

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Summary

Introduction

Aptamer is derived from one Latin and one Greek word combinations: “aptus,” which means “fit,” and “meros” meaning “particle” [1]. 30 Cancer Management and Therapy has low molecular weight (5–40 kDa) and three-dimensional (3D) structure with a high binding affinity against target protein. SELEX is a consecutive processes starting with binding of target with random sequence of oligonucleotide library, washing and elution of unbound oligonucleotides, amplification of 3D structure oligonucleotides against the target epitope via polymerase chain reaction (PCR), selection of aptamers with high binding affinity and specificity, and modifications of novel aptamers to increase stability and function [3]. Aptamers are similar to antibodies due to their binding affinity to target molecule, they have a number of advantages such as small and low complexity with low immunogenic activity, high stability, high affinity and specificity for their targets, and easy to synthesize and modify in vitro [4]

SELEX method
Aptamer-based drugs for cancer therapy
Cell-specific targets for aptamer-based therapeutic strategies
Pegaptanib
A9g RNA aptamer
HPV16 E6 (F5) aptamer
ErbB targeting aptamers
A30 aptamer
OPN aptamer
NAS-24 aptamer
YJ-1 aptamer
A-P50 aptamer
2.1.10. AP273 AFP aptamer
Immunomodulatory aptamers in the treatment of different solid tumors
Targeted drug delivery in cancer therapy via aptamers
Prostate-specific membrane antigen
Tenascin-C
Nucleolin
Mucin-1
Protein tyrosine kinase 7
Epidermal growth factor receptor
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