Biotinylation
Biotinylation — The process of attaching biotin to a peptide or protein, enabling detection, purification, or immobilization through the strong biotin-streptavidin interaction.
What Is Biotinylation?
Biotinylation is the covalent attachment of biotin (vitamin B7) to a peptide, enabling ultra-sensitive detection and capture through the biotin-streptavidin interaction (Kd ~10⁻¹⁵ M, the strongest known non-covalent biological interaction). Biotinylated peptides are essential tools for binding assays, biopanning, and peptide pull-down experiments.
Applications
- Pull-down assays: Biotinylated peptide immobilized on streptavidin beads captures binding partners from cell lysates
- ELISA capture: Streptavidin-coated plates bind biotinylated peptides in oriented fashion
- Imaging: Fluorescent streptavidin detects biotinylated peptides on cells or tissues
- Synthesis: Biotin-NHS added on-resin to N-terminus or Lys side chain during SPPS
Frequently Asked Questions
What is Biotinylation?
The process of attaching biotin to a peptide or protein, enabling detection, purification, or immobilization through the strong biotin-streptavidin interaction.
Why is Biotinylation important in peptide research?
Biotinylation is a fundamental concept in modification as it relates to peptide science. It directly influences experimental design, compound characterization, and the reliability of research outcomes across biochemistry and molecular biology disciplines.