Screening nonspecific interactions of peptides without background interference

Citation

Keefe, Andrew J.; Caldwell, Kyle B.; Nowinski, Ann K.; White, Andrew D.; Thakkar, Amit; & Jiang, Shaoyi (2013). Screening nonspecific interactions of peptides without background interference. Biomaterials, 34(8), 1871-1877.

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.

Keyword(s)

Adsorption
Amino Acid Sequence
Animals
Cattle
Fibrinogen
glass
Microscopy, Fluorescence
Microspheres
Molecular Sequence Data
Peptide Library
Peptides
Photoelectron Spectroscopy
Protein Binding
Surface Properties

Reference Type

Journal Article

Secondary Title

Biomaterials

Author(s)

Keefe, Andrew J.
Caldwell, Kyle B.
Nowinski, Ann K.
White, Andrew D.
Thakkar, Amit
Jiang, Shaoyi

Year Published

2013

Volume Number

34

Issue Number

8

Pages

1871-1877

ISSN/ISBN

1878-5905

DOI

10.1016/j.biomaterials.2012.11.014