Authors: G.A. Kuzmicheva, A.M. Eroshkin, V.A. Potemkin, V.A. Petrenko
Affilation: Auburn University, United States
Pages: 442 - 445
Keywords: landscape phage, nanoparticles
Phage peptide libraries proved to be invaluable source of the ligands specifically binding numerous analytes. Diversity and repertoir of the libraries are critical for the successful selection of ligands. In landscape libraries guest peptides are fused to each of 4000 copies of the major coat protein pVIII and form unique binding “landscapes” on the phage surface, so that the whole phage particle operates as a bioselective nanodevice with genetically determined regular structure. To explore how amino acids neighboring a guest peptide in the pVIII protein influence a binding ability of the phage nanoparticle, the phage that binds ß-galactosidase and carries peptide ADTFAKSMQ at the N-terminus of pVIII, was used as a model. A collection of phages carrying ADTFAKSMQ peptides and random mutations distant from the insert, have been constructed. We found that the mutations in the pVIII can improve or completely destroy the phage’s affinity towards ß-galactosidase. These features correlate with the common charge formed by mutated amino acids. Influence of the guest peptide on the diversity of mutations in the neighboring area of pVIII was also revealed. Based on these data, the concept of novel SPLIT landscape libraries as a new source of phage nanoparticles with modulated diversity of displayed peptides is formulated and discussed.