Affiliation:
1. Department of General Chemistry, Belarusian State Medical University, Minsk, Belarus
Abstract
Aims:
The aim of this study was to create a new version of the PentaFOLD algorithm and to test its performance
experimentally in several proteins and peptides.
Background:
Synthetic vaccines can cause production of neutralizing antibodies only in case if short peptides form the
same secondary structure as fragments of full-length proteins. The PentaFOLD 3.0 algorithm was designed to check stability
of alpha helices, beta strands, and random coils using several propensity scales obtained during analysis of 1730 3D structures of proteins.
Objective:
The algorithm has been tested in the three peptides known to keep the secondary structure of the corresponding
fragments of full-length proteins: the NY25 peptide from the Influenza H1N1 hemagglutinin, the SF23 peptide from the
diphtheria toxin, the NQ21 peptide from the HIV1 gp120; as well as in the CC36 peptide from the human major prion
protein.
Method:
Affine chromatography for antibodies against peptides accompanied by circular dichroism and fluorescence spectroscopy were used to check the predictions of the algorithm.
Result:
Immunological experiments showed that all abovementioned peptides are more or less immunogenic in rabbits. The
fact that antibodies against the NY25, the SF23, and the NQ21 form stable complexes with corresponding full-length proteins has been confirmed by affine chromatography. The surface of SARS CoV-2 spike receptor-binding domain interacting
with hACE2 has been shown to be unstable according to the results of the PentaFOLD 3.0.
Conclusion:
The PentaFOLD 3.0 algorithm (http://chemres.bsmu.by/PentaFOLD30.htm) can be used with the aim to design
vaccine peptides with stable secondary structure elements.
Publisher
Bentham Science Publishers Ltd.
Subject
Biochemistry,General Medicine,Structural Biology
Cited by
4 articles.
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