| Literature DB >> 16369689 |
Yun-Gon Kim1, Chang-Soo Lee, Woo-Jae Chung, Eun-Mi Kim, Dong-Sik Shin, June-Hyung Kim, Yoon-Sik Lee, Junho Chung, Byung-Gee Kim.
Abstract
Lipopolysaccharide (LPS)-binding peptides were enriched by using epoxy beads as a novel support to immobilize LPS for a phage displayed peptide library screening. The sequence of Phe-Ala-Pro-Trp (FAPW) was the most significant consensus motif of 10 selected clones, and Pro-Phe (PF) was the key dipeptide for binding at the apex of the loop to form a characteristic structure of CXXPFXXXC. Moreover, AWLPWAK, one of the highly conserved heptamer peptides, could detect specifically Gram-negative bacteria via a whole cell binding test at 10(6) cells ml(-1).Entities:
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Year: 2006 PMID: 16369689 DOI: 10.1007/s10529-005-4950-4
Source DB: PubMed Journal: Biotechnol Lett ISSN: 0141-5492 Impact factor: 2.461