Antisense Peptide Technology for Diagnostic Tests and Bioengineering Research

Abstract

Antisense peptide technology (APT) is based on a useful heuristic algorithm for rational peptide design. It was deduced from empirical observations that peptides consisting of complementary (sense and antisense) amino acids interact with higher probability and affinity than the randomly selected ones. This phenomenon is closely related to the structure of the standard genetic code table, and at the same time, is unrelated to the direction of its codon sequence translation. The concept of complementary peptide interaction is discussed, and its possible applications to diagnostic tests and bioengineering research are summarized. Problems and difficulties that may arise using APT are discussed, and possible solutions are proposed. The methodology was tested on the example of SARS-CoV-2. It is shown that the CABS-dock server accurately predicts the binding of antisense peptides to the SARS-CoV-2 receptor binding domain without requiring predefinition of the binding site. It is concluded that the benefits of APT outweigh the costs of random peptide screening and could lead to considerable savings in time and resources, especially if combined with other computational and immunochemical methods.

Peptide-Integrated Superparamagnetic Nanoparticles for the Identification of Epitopes from SARS-CoV-2 Spike and Nucleocapsid Proteins

“…On the other hand, the serodiagnosis still needs improvement to guaranty appropriate sensitivity and specificity. Furthermore, the identification of epitopes by bioinformatics has been a useful tool for the development of antigens to detect specific antibodies against SARS-CoV-2. ,,− However, the epitope predictions made so far from SARS-CoV-2 proteins are essentially linear, based on the primary structure of these proteins. ,,, This can lead to cross-reactions due to the high similarity degree between protein primary sequences of other coronaviruses, which would impair detection. Moreover, most antigenic determinants recognized by B cells and antibodies are conformational epitopes because the regions of interaction between antigen and antibody involve amino acids that are not continuous in the primary sequence of protein but assemble in the protein when it folded, mimicking the epitope region as in the structural conformation of the protein .…”