Maltose neopentyl glycol-3 (MNG-3) analogues for membrane protein study

Research output: Contribution to journalJournal articleResearchpeer-review

  • Kyung Ho Cho
  • Mohd Husri
  • Anowarul Amin
  • Kamil Gotfryd
  • Ho Jin Lee
  • Juyeon Go
  • Jin Woong Kim
  • Løland, Claus Juul
  • Lan Guan
  • Bernadette Byrne
  • Pil Seok Chae

Detergents are typically used to both extract membrane proteins (MPs) from the lipid bilayers and maintain them in solution. However, MPs encapsulated in detergent micelles are often prone to denaturation and aggregation. Thus, the development of novel agents with enhanced stabilization characteristics is necessary to advance MP research. Maltose neopentyl glycol-3 (MNG-3) has contributed to >10 crystal structures including G-protein coupled receptors. Here, we prepared MNG-3 analogues and characterised their properties using selected MPs. Most MNGs were superior to a conventional detergent, n-dodecyl-β-d-maltopyranoside (DDM), in terms of membrane protein stabilization efficacy. Interestingly, optimal stabilization was achieved with different MNG-3 analogues depending on the target MP. The origin for such detergent specificity could be explained by a novel concept: compatibility between detergent hydrophobicity and MP tendency to denature and aggregate. This set of MNGs represents viable alternatives to currently available detergents for handling MPs, and can be also used as tools to estimate MP sensitivity to denaturation and aggregation.

Original languageEnglish
JournalThe Analyst
Issue number9
Pages (from-to)3157-63
Number of pages7
Publication statusPublished - 2015

ID: 137623574