Solubility improvement of an anthrax toxin peptide inhibitor by rational amino acid randomization.

Abstract:

:We previously described a potent anthrax toxin inhibitor, based on a phage-library-selected peptide sequence, synthesized as a tetra-branched molecule on a lysine core and further modified for improvement of activity [Pini et al., Biochem. J., 2006, 395, 157]. This branched peptide had very low solubility because of several hydrophobic residues in the peptide sequence. This complicated molecule purification and manufacturing. Here we report a rational modification of the peptide sequence, obtained by construction and selection of several mini libraries of branched peptides, containing sequences randomized in non crucial positions of the original peptide. Mini libraries were screened for solubility and inhibitory activity. This procedure enabled us to obtain a new peptide with a better solubility and identical inhibitory activity.

journal_name

Protein Pept Lett

authors

Pini A,Brunetti J,Falciani C,Fabbrini M,Bracci L

doi

10.2174/092986608784966958

subject

Has Abstract

pub_date

2008-01-01 00:00:00

pages

562-6

issue

6

eissn

0929-8665

issn

1875-5305

journal_volume

15

pub_type

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