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Updated: Feb 10, 2026

A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
Published on: October 1, 2009
Low Fouling Protein Detection in Complex Biological Media Supported by a Designed Multifunctional Peptide
Nianzu Liu1, Ni Hui1,2, Jason J Davis3
1Key Laboratory of Sensor Analysis of Tumor Marker, Ministry of Education, College of Chemistry and Molecular Engineering , Qingdao University of Science and Technology , Qingdao 266042 , China.
Abstract:
The construction of sensitive and selective biosensors capable of detecting specific targets in complex biological samples remains a challenge highly relevant to a range of sensor/diagnostic applications. Herein, we have utilized a multifunctional peptide to present an interface that supports the very specific recruitment of targets from serum. The novel peptide sequence designed contains an anchoring domain (CPPPP-), an antifouling domain (-NQNQNQNQDHWRGWVA), and a human immunoglobulin G (IgG) recognition domain (-HWRGWVA), and the whole peptide was designed to be antifouling. These were integrated into polyaniline nanowire arrays in supporting the quantification of IgG (with a limit of detection of 0.26 ng mL-1) in neat serum and real clinical samples. The strategy of utilizing multisegment peptide films to underpin highly selective target recruitment is, of course, readily extended to a broad range of targets for which an affinity sequence can be generated.
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