SPRi determination of inter-peptide interaction by using 3D supramolecular co-assembly polyrotaxane film

Yanmei Wang, Chenxuan Wang, Zhiqiang Cheng, Dongdong Zhang, Shaopeng Li, Lusheng Song, Wenfei Zhou, Mo Yang, Zhiyou Wang, Zheng Zheng, Baohang Han, Chen Wang, Yanlian Yang, Jinsong Zhu

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


Accurate measurement of inter-peptide interactions is beneficial for in-depth understanding disease-related protein folding and peptide aggregation, and further for designing and selecting potential peptide drugs to the target antigen. Herein, we demonstrate a 3D polyrotaxane (PRX) surface for detecting peptides interactions by surface plasmon resonance imaging (SPRi). This surface is supramolecular self-assembly monolayer (SAM) structure fabricated by threading α-cyclodextrans (α-CD) through a linear polyethylene glycol (PEG) chain fixed on gold chip surface to form pseudopolyrotaxane, and further capping the pseudopolyrotaxane with bulky terminated group to form PRX film. The hydroxyl groups of α-CD can provide more active sites to increase molecules immobilization density, and PEG chain has unique protein non-fouling feature. We chose Alzheimer's disease marker β-amyloid 40 (Aβ40) as model peptide, and detected the interaction between it and its inhibitors KLVFFK6 by SPRi. As a striking result, the specific adsorption of KLVFFK6 solution at the concentration of 352μM on Aβ40-PRX was 700RU, whereas PEG SAM surface gave no significant binding. Interaction between other lower molecular weight peptides was detected via PRX surface, and the relatively weak interactions (KD=1.73×10-4M) between LPFFD (Mw=0.6kDa) and amylin20-29 (Mw=1.0kDa) are successfully detected.

Original languageEnglish (US)
Pages (from-to)338-344
Number of pages7
JournalBiosensors and Bioelectronics
StatePublished - Apr 5 2015
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology
  • Biophysics
  • Biomedical Engineering
  • Electrochemistry


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