Screening nonspecific interactions of peptides without background interference

Abstract The need to discover new peptide sequences to perform particular tasks has lead to a variety of peptide screening methods: phage display, yeast display, bacterial display and resin display. These are effective screening methods because the role of background binding is often insignificant....

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Bibliographic Details
Published in:Biomaterials 2013-03, Vol.34 (8), p.1871-1877
Main Authors: Keefe, Andrew J, Caldwell, Kyle B, Nowinski, Ann K, White, Andrew D, Thakkar, Amit, Jiang, Shaoyi
Format: Article
Language:English
Subjects:
Adsorption
Advanced Basic Science
Amino Acid Sequence
Animals
Bacteria
Binding
Cattle
Charge
Dentistry
Fibrinogen - metabolism
Glass - chemistry
Microscopy, Fluorescence
Microspheres
Molecular Sequence Data
Peptide
Peptide Library
Peptide screening
Peptides
Peptides - analysis
Peptides - chemistry
Peptides - metabolism
Peptides - pharmacology
Photoelectron Spectroscopy
Protein adsorption
Protein Binding - drug effects
Screening
Segregations
Surface modification
Surface Properties
Surgical implants
Yeast
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Summary:Abstract The need to discover new peptide sequences to perform particular tasks has lead to a variety of peptide screening methods: phage display, yeast display, bacterial display and resin display. These are effective screening methods because the role of background binding is often insignificant. In the field of nonfouling materials, however, a premium is placed on chemistries that have extremely low levels of nonspecific binding. Due to the presence of background binding, it is not possible to use traditional peptide screening methods to select for nonfouling chemistries. Here, we developed a peptide screening method, as compared to traditional methods, that can successfully evaluate the effectiveness of nonfouling peptide sequences. We have tested the effect of different peptide lengths and chemistries on the adsorption of protein. The order of residues within a single sequence was also adjusted to determine the effect of charge segregation on protein adsorption.
ISSN:0142-9612
1878-5905
DOI:10.1016/j.biomaterials.2012.11.014