Molecular Recognition at Protein Surface in Solution and Gas Phase: Five VEGF Peptidic ligands Show Inverse Affinity When Studied by NMR and CID-MS

作者：Dyachenko Andrey; Goldflam Michael; Vilaseca Marta; Giralt Ernest^*

来源：Biopolymers, 2010, 94(6): 689-700.

DOI：10.1002/bip.21462

• protein-ligand interactions
• molecular recognition noncovalent interactions
• gas phase interactions mass spectrometry
• vascular endothelial growth factor (VEGF)

Protein-protein interactions comprise of collection of molecular recognition events that take place at protein surfaces A better understanding of the mechanism behind these interactions would provide deeper insight into the nature of many diseases, caused by the malfunction of protein networks, and contribute to design of molecules for efficient modulating of these interactions One major factor in molecular recognition mechanism is interaction of reacting species with aqueous media Thus, comparative study of noncovalent complex behavior in solution and gas phase can provide valuable information about the role of the solvent Here examined interactions of vascular endothelial growth factor (VEGF) protein with five peptide ligands of the same molecular weight but with different affinities Interactions of VEGF with ligands in solution were studied by ITC and NMR, and K(D)s were determined Gas phase stability was addressed using CID-MS approach The energy transfer model was taken and adapted for the calculation of binding energy gas phase, affinity to VEGF The results indicate that the if ranking,of Peptides in terms of affinity in solution is reversed compared with the gas phase ranking This observation opens up a vast field for the future study of the system, and the determination and characterization of factors,

• 出版日期2010