Peptides isolated from random peptide libraries on phage elicit a neutralizing anti‐HIV‐1 response: analysis of immunological mimicry
نویسندگان
چکیده
منابع مشابه
Puzzling Peptides from a Phage Display Library
The commercial availability of random peptide libraries displayed on the M13 phage is increasing their use forstudies on epitope identification, enzyme inhibitors, receptor ligands, etc. In this study two experimentswhere planned for selection of peptides. First with sheep antibodies, the positive selector was IgG, preparedon Protein G column from a pool of 11 sheeps immunized...
متن کاملErythromycin resistance peptides selected from random peptide libraries.
Translation of a 5-codon mini-gene encoded in Escherichia coli 23 S rRNA was previously shown to render cells resistant to erythromycin (Tenson, T., DeBlasio, A., and Mankin, A. S. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 5641-5646). Erythromycin resistance was mediated by a specific interaction of the 23 S rRNA-encoded pentapeptide with the ribosome. In the present study, peptides conferring...
متن کاملIdentifying reactive peptides from phage-displayed libraries.
Phage display enables the synthesis, selection, and screening of large, polypeptide libraries (>1 × 10(10) different members). Selections from such libraries can identify binding partners to essentially any desired target (Sarikaya et al., Annu Rev Mater Res 34:373-408, 2004; Deutscher, Chem Rev 110:3196-3211, 2010). Peptides with affinity or reactivity to small molecule probes are attractive f...
متن کاملIsolation of peptides from phage-displayed random peptide libraries that interact with the talin-binding domain of vinculin.
Peptides isolated from combinatorial libraries typically interact with, and thus help to characterize, biologically relevant binding domains of target proteins. To characterize the binding domains of the focal adhesion protein vinculin, vinculin-binding peptides were isolated from two phage-displayed random peptide libraries. Altogether, five non-similar vinculin-binding peptides were identifie...
متن کاملApparent heterogeneity in the pIII-peptide fusion protein in single-phage clones isolated from peptide libraries.
Ligand homogeneity is an important issue in affinity chromatography. Using phages expressing peptides on the pIII protein, a heterogeneity in the binding of monoclonal phages was observed during affinity chromatography on supermacroporous cryogels. Fractions with different apparent binding affinities could be separated by stepwise elution. When these different fractions were re-applied, the res...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Immunology
سال: 1996
ISSN: 0019-2805,1365-2567
DOI: 10.1046/j.1365-2567.1996.d01-772.x