BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 1337

Peptides:

Sequences

FVRPFPL(6)
FVRPFAL(4)
FVRPYAP(2)
FPRTIAP(1)
DIRTQRE(4)
DIRTQTR(2)
DIRATQA(2)
ATPLWLK(5)
ATPTQRE(3)
ATPLYLR(2)
TLWDLIP(5)
TLWSFMP(3)
TLWVPSR(2)
TLTTLTN(2)
TLTFFHR(2)
TYLPWPA(5)
TYLPWPP(2)
TYLRARL(3)
TYPFAPW(2)

Sequences Features:

Motif:

TLW, VRP

Unique Sequence Number:

Experimental Method:

Phage display (common panning)

Sequencing Platform:

Sequencing Method:

Sanger sequencing

Rounds of Panning:

Reference:

PMID: 21278676

Target Name:

Modified helix 31 of bacterial 16S ribosomal RNA

Template Name:

Not determined.

Structure of Target-Template Complex:

Not determined.

Structure of Target-Peptide Complex:

Not determined.

Library Name:

Ph.D.-7 phage display library (X7)

Affinity Measurement Method:

Affinity Measurement Description:

Brief Description:

Duplicate samples of h31 on magnetic beads were employed for selection. For each sample of h31, 100 isolates were sequenced. Phage isolates were sequenced after the third round of selection against wild-type modified h31 on streptavidin-coated beads.

BiopanningDataSet Comments:

Two hundred phage isolates were sequenced after the third round of selection against wild-type modified h31 on streptavidin-coated beads. Only peptide sequences with repeated sequences or common motifs are shown. Several of the peptides exhibited moderate affinity (in the high nM to low μM range) to modified helix 31 in biophysical assays, including surface plasmon resonance (SPR), and were also shown to bind 30S ribosomal subunits. These peptides also inhibited protein synthesis in cell-free translation assays.

Curator:

Curation Date:

0000-00-00

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