Dec 14, 2011

Amino acid-anticodon binding specificity: rationale for a new class of therapeutic agent

Drug Discovery Today
Marvin S Melzer

Abstract

In this article a new class of anticancer and antiviral drugs is discussed. These new drugs consist of small di- and tri-peptides, designed to bind to single-stranded (ss) regions that are crucial for the expression of genes such as the c-myc oncogene in cancers and start sites (and other ss regions) of viral pathogenic genes. The components (i.e. the amino acids and the sequences they form) of these peptides could be dictated by the specific binding of amino acids to their ss anticodons in tRNA. Cancer cell viability depends on the continued overexpression of the c-myc oncogene, and thus this gene is a target of opportunity for anticancer agents. Sharply reducing the overexpression of c-myc leads to the death of cancer cells. To achieve this end the following rationale is suggested: crucial regions of the c-myc promoters (to which activating proteins must bind for expression to occur) are single stranded and thus strongly resemble the anticodon loop of tRNA. It was found that amino acids chemically bind to their cognate tRNA anticodons. Regarding the ss regions of c-myc as a series of adjacent 'anticodons', di- and tri-peptides are proposed to be aligned to their cognate 'anticodons' in the proper order. For example, if the ss...Continue Reading

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Citations

Mentioned in this Paper

Antineoplastic Agents
Human Papillomavirus
Pathogenic Organism
DNA-Directed RNA Polymerase
RNA Polymerase Assembly Pathway
Simplexvirus
Vaccines
Amino Acids, I.V. solution additive
MT-TA gene
Triplet Codon-amino Acid Adaptor Activity

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