Nucleic Acid and Peptide Aptamers: Fundamentals and Bioanalytical Aspects

Abstract

In recent years new nucleic acid and protein-based combinatorial molecules have attracted the attention of researchers working in various areas of science, ranging from medicine to analytical chemistry. These molecules, called aptamers, have been proposed as alternatives to antibodies in many different applications. The aim of this Review is to illustrate the peculiarities of these combinatorial molecules which have initially been explored for their importance in molecular medicine, but have enormous potential in other biotechnological fields historically dominated by antibodies, such as bioassays. A description of these molecules is given, and the methods for their selection and production are also summarized. Moreover, critical aspects related to these molecules are discussed.

Perspectives in Glycomics and Lectin Engineering

“…Such proteins will be peptide aptamers with a lectin-like affinity to recognise various forms of glycans. A term peptide aptamer was coined by Colas et al in 1996 (79) and is defined as a combinatorial protein molecule having a variable peptide sequence, with an affinity for a given target protein, displayed on an inert, constant scaffold protein (80). Construction of various !…”

“…Moreover, when a small PLA will be immobilised on the surface of various bioanalytical devices, a higher density of biorecognition element can enhance sensitivity of detection, while suppressing non-specific interactions and lowering background signals (80). Peptide aptamers are produced by protein engineering from high-complexity combinatorial libraries with appropriate isolation/selection methods (82,80,81).…”

“…Peptide aptamers are produced by protein engineering from high-complexity combinatorial libraries with appropriate isolation/selection methods (82,80,81). Thus, a need to have knowledge of the protein structure and the mechanism behind binding is not necessary.…”

Protein-Peptide Interactions Revolutionize Drug Development

“…They are combinatorial protein molecules (Figure 3), which consist of a variable peptide loop attached at both ends to an inert, constant scaffold protein [58][59][60]. The scaffold should preferable be small, composed of a single chain, and with a highly stable structure [61].…”

“…The scaffold should preferable be small, composed of a single chain, and with a highly stable structure [61]. The choice between different scaffolds such as thioredoxin A (TrxA) [62], staphylococcus nuclease [63], human stefin A [64], and green fluorescent protein [65] is made by taking into account the intended use of the peptide [59]. Scaffold structures restrict the conformation of the peptide such that the loop can only adopt a discrete shape from the conformational space available to it.…”