Membrane Protecting Sequences and New Antimicrobial Peptides Identified through the Screening of Synthetic Peptide Combinatorial Libraries Book Chapter

Blondelle, SE, Houghten, RA. (1994). Membrane Protecting Sequences and New Antimicrobial Peptides Identified through the Screening of Synthetic Peptide Combinatorial Libraries . 5 509-516. 10.1016/B978-0-12-194710-1.50062-X

cited authors

  • Blondelle, SE; Houghten, RA

authors

abstract

  • This chapter explores the membrane protecting sequences and new antimicrobial peptides identified through the screening of synthetic peptide combinatorial libraries. Two tetrapeptide libraries, one N-acetylated and the other not, made up of the 20 naturally occurring L-amino acids, 19 D amino acids, and 19 other amino acids commonly used in peptide synthesis, were prepared. Each synthetic peptide combinatorial library (SPCL) is composed of tetrapeptides having one position individually defined, while the remaining positions are made up of mixtures of amino acids. The chapter presents this tetrapeptide library for the development of new antimicrobial peptides effective against Escherichia coli (E. coli). In a study described in the chapter, the two tetramer SPCLs were screened for inhibition of E. coli growth in a microdilution assay. The IC50 s was determined for each of the peptide mixtures. The non-N-acetylated peptide mixtures were found to be more active than the corresponding N-acetylated ones. The peptide mixture ZZZ–NH2 was found to exhibit the highest activity. This peptide mixture was chosen to carry out an iterative selection process. © 1994 ACADEMIC PRESS, INC.

publication date

  • January 1, 1994

Digital Object Identifier (DOI)

start page

  • 509

end page

  • 516

volume

  • 5