Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2

Petr Pompach, Cristina M. Viola, Jelena Radosavljević, Jingjing Lin, Jiří Jiráček, Andrzej M. Brzozowski, Irena Selicharová*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Structural details of changes accompanying interaction between insulin-related hormones and their binding partners are often enigmatic. Here, cross-linking/mass spectrometry could complement structural techniques and reveal details of these protein-protein interfaces. We used such approach to clarify missing structural description of the interface in human insulin-like growth factor (IGF-1): Drosophila melanogaster imaginal morphogenesis protein-late 2 protein (Imp-L2) complex which we studied previously by X-ray crystallography. We crosslinked these proteins by heterobifunctional cross-linker sulfosuccinimidyl 4,4′-azidopentanoate (Sulfo-SDA) for the subsequent mass spectrometry (MS) analysis. The MS analysis revealed IGF-1:Imp-L2 interactions which were not resolved in the crystal structure of this assembly, and they converged with X-ray results, indicating the importance of the IGF-1 N-terminus interaction with the C-terminal (185–242) part of the Imp-L2 for stability of this complex. Here, we also showed the advantage and reliability of MS approach in solving details of protein-protein interactions that are too flexible for solid state structural methods.

Original languageEnglish
Article number695
Pages (from-to)1-10
Number of pages10
JournalFrontiers in Endocrinology
Publication statusPublished - 9 Oct 2019

Bibliographical note

© 2019 Pompach, Viola, Radosavljević, Lin, Jiráček, Brzozowski and Selicharová.


  • cross-linking
  • diazirine ring
  • IGF-1
  • Imp-L2
  • mass spectrometry

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