Predicting the right spacing between protein immobilization sites on self-assembled monolayers to optimize ligand binding

Javier Batista Perez, Deependra Tyagi, Mo Yang, Loany Calvo, Rolando Perez, Ernesto Moreno, Jinsong Zhu

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

Abstract Self-assembled monolayers designed to immobilize capture antibodies are usually prepared using a mixture of functional and inactive linkers. Here, using low molar ratios (1:1 to 1:100) of the two linkers resulted in loss of binding capability of the anti-EGFR (epidermal growth factor receptor) antibody nimotuzumab, as assessed by surface plasmon resonance imaging. We then developed a simple theoretical model to predict the optimal surface density of the functional linker, taking into account the antibody size and linker diameter. A high (1:1000) dilution of the functional linker yielded the best results. As an advantage, this approach does not require chemical modification of the protein.

Original languageEnglish
Article number12078
Pages (from-to)133-135
Number of pages3
JournalAnalytical Biochemistry
Volume484
DOIs
StatePublished - 24 Jun 2015
Externally publishedYes

Keywords

  • Antibody
  • Nimotuzumab
  • Protein immobilization
  • Self-assembled monolayer
  • Surface plasmon resonance
  • Theoretical model

Fingerprint

Dive into the research topics of 'Predicting the right spacing between protein immobilization sites on self-assembled monolayers to optimize ligand binding'. Together they form a unique fingerprint.

Cite this