Monolayers assembled from a glycolipid biosurfactant from Pseudozyma (Candida) antarctica serve as a high-affinity ligand system for immunoglobulin G and M

Biotechnol Lett. 2007 Jun;29(6):865-70. doi: 10.1007/s10529-007-9335-4. Epub 2007 Mar 7.

Abstract

A carbohydrate ligand system has been developed which is composed of self-assembled monolayers (SAMs) of mannosylerythritol lipid-A (MEL-A) from Pseudozyma antarctica, serving for human immunoglobulin G and M (HIgG and HIgM). The estimated binding constants from surface plasmon resonance (SPR) measurement were Ka = 9.4 x 10(6) M(-1) for HIgG and 5.4 x 10(6) M(-1) for HIgM, respectively. The binding site was not in the Fc region of immunoglobulin but in the Fab region. Large amounts of HIgG and HIgM bound to MEL-A SAMs were directly observed by atomic force microscopy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Candida / chemistry*
  • Glycolipids / chemistry
  • Glycolipids / metabolism*
  • Humans
  • Immunoglobulin G / chemistry
  • Immunoglobulin G / metabolism*
  • Immunoglobulin M / chemistry
  • Immunoglobulin M / metabolism*
  • Ligands
  • Microscopy, Atomic Force
  • Models, Biological
  • Molecular Structure
  • Protein Binding
  • Surface Plasmon Resonance
  • Surface-Active Agents / chemistry
  • Surface-Active Agents / metabolism

Substances

  • Glycolipids
  • Immunoglobulin G
  • Immunoglobulin M
  • Ligands
  • Surface-Active Agents
  • mannosylerythritol lipid