Title
May heterocyclic γ‐peptides provide polyfunctional platforms for synthetic glycocluster construction?
Author
Matthieu Simon, Lamiaa M. A. Ali, Khaled El Cheikh, Julie Aguesseau, Magaly Gary-Bobo, Marcel Garcia, Alain Morère, Ludovic Thierry Maillard
Year
2018
Journal
Chemistry A European Journal
Abstract
Sugars play key roles in many molecular and cellular communication processes involving a family of proteins named lectins. The low affinity associated with sugar recognition is generally counterbalanced by the multivalent nature of the interaction. While many polyglycosylated architecture have been described, only few studies focused on the impact of topology variations of the multivalent structures on the interaction with lectin proteins. One major interest of our group concerns the design of new highly predictable and stable molecular pseudo‐peptide architecture for therapeutic applications. In such a context, we described a class of constrained heterocyclic γ‐amino acids built around a thiazole ring, named ATCs. ATC oligomers are helical molecules resulting from the formation of a highly stable C9 hydrogen‐bonding pattern. Following our program, we herein address the potential of ATC oligomers as tunable scaffold to develop original multivalent glyco‐clusters.
Instrument
J-815
Keywords
Circular dichroism, Secondary structure, Protein folding, Chemical stability, Biochemistry