Selection of Peptides Targeting Helix 31 of Bacterial 16S Ribosomal RNA by Screening M13 Phage-Display Libraries 英文参考文献.docVIP
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Selection of Peptides Targeting Helix 31 of Bacterial 16S Ribosomal RNA by Screening M13 Phage-Display Libraries 英文参考文献
Molecules 2011, 16, 1211-1239; doi:10.3390/molecule
OPEN ACCESS
molecules
ISSN 1420-3049
/journal/molecules
Article
Selection of Peptides Targeting Helix 31 of Bacterial 16S
Ribosomal RNA by Screening M13 Phage-Display Libraries
Tek N. Lamichhane 1,2,?,?, N. Dinuka Abeydeera 1,§,?, Anne-Cécile E. Duc 1,||,
Philip R. Cunningham 2 and Christine S. Chow 1,*
1
Department of Chemistry, Wayne State University, Detroit, MI 48202, USA
2
Department of Biological Sciences, Wayne State University, Detroit, MI 48202, USA
?
Current address: Intramural Research Program, NICHD, NIH, Bethesda, MD 20892, USA
§
Current address: Department of Chemistry, Texas AM University, College Station, TX 77843, USA
||
Current address: Immune Cell Development and Host Defense Program, Fox Chase Cancer Center,
333 Cottman Avenue, Philadelphia, PA 19111, USA
?
These authors contributed equally to this work.
* Author to whom correspondence should be addressed; E-Mail: csc@;
Tel: +1-313-577-2594; Fax: +1-313-577-8822.
Received: 5 January 2011; in revised form: 24 January 2011 / Accepted: 25 January 2011 /
Published: 28 January 2011
Abstract: Ribosomal RNA is the catalytic portion of ribosomes, and undergoes a variety
of conformational changes during translation. Structural changes in ribosomal RNA can be
facilitated by the presence of modified nucleotides. Helix 31 of bacterial 16S ribosomal
RNA harbors two modified nucleotides, m2G966 and m5C967, that are highly conserved
among bacteria, though the degree and nature of the modifications in this region are
different in eukaryotes. Contacts between helix 31 and the P-site tRNA, initiation factors,
and ribosomal proteins highlight the importance of this region in translation. In this work, a
heptapeptide M13 phage-display library was screened for ligands that target the wild-type,
naturally modified bacterial helix 31. Several peptides, including TYLPWPA, CVRPFAL,
TLWDLIP, FVRPFPL, ATPLWLK, and
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