Author: Lubomir Vezenkov

A Review from the team just published in J Mater Chem B!!! Inorganic polymerization: an attractive route to biocompatible hybrid hydrogels

Congratulations for the first paper of Titouan!

J. Mater. Chem. B, 2018,6, 3434-3448,  doi 10.1039/C8TB00456K

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Titouan is the first author of a really nice, well illustrated and comprehensive review about hybrid hydrogels, (i.e. defined by the coexistence of organic and inorganic moieties in water). Inorganic polymerization, i.e. the sol–gel process, is one of the main techniques leading to hybrid hydrogels. In addition, the mild reaction conditions make this process very promising for the preparation of water-containing materials and their bio-applications.

Have a look at J Mater Chem B !

J. Mater. Chem. B, 2018,6, 3434-3448,  doi 10.1039/C8TB00456K

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Inorganic polymerization: an attractive route to biocompatible hybrid hydrogels

J. Mater. Chem. B, 2018,6, 3434-3448,  doi 10.1039/C8TB00456K

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Abstract

As an intermediate state between liquid and solid materials, hydrogels display unique properties, opening a wide scope of applications, especially in the biomedical field. Organic hydrogels are composed of an organic network cross-linked via chemical or physical reticulation nodes. In contrast, hybrid hydrogels are defined by the coexistence of organic and inorganic moieties in water. Inorganic polymerization, i.e. the sol–gel process, is one of the main techniques leading to hybrid hydrogels. The chemoselectivity of this method proceeds through hydrolysis and condensation reactions of metal oxide moieties. In addition, the mild reaction conditions make this process very promising for the preparation of water-containing materials and their bio-applications.

Can Heterocyclic γ-Peptides Provide Polyfunctional Platforms for Synthetic Glycocluster Construction?

Chemistry. 2018 May 30. doi: 10.1002/chem.201802032

Simon M, Ali LMA, El Cheikh K, Aguesseau J, Gary-Bobo M, Garcia M, Morère A, Maillard LT.

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 architectures have been described, only a 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 architectures 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 scaffolds for the development of original multivalent glycoclusters.

Structure based drug design

Structure Based Drug Design

We develop several projects related to the characterization and inhibition of molecular interactions between proteins and protein-ligand.

Based on molecular modeling studies of protein-protein or protein-ligand interactions, our first step is to design pharmacophore constraints to orient the design of putative inhibitor candidates. In collaboration with chemists, the most suitable scaffold (foldamer, chemical molecule and peptide) is selected and candidates are synthetized. Then, after purification of functional proteins, we carry out protein-protein and protein-ligand interaction studies by biophysics to evaluate the inhibitory potency of compounds.

CONTACT

Alain Chavanieu
Alain Chavanieu
Ludovic Maillard
Ludovic Maillard
Sébastien Estran
Sébastien Estran

Selectivity Modulation and Structure of α/aza-β3 Cyclic Antimicrobial Peptides

Chemistry 2018 Apr 20;24(23):6191-6201. doi: 10.1002/chem.201800152. Epub 2018 Mar 26.

 Simon MLaurencin M, Fleury Y, Baudy-Floc’h M, Bondon A, Legrand B.

Abstract

Potent and selective antimicrobial cyclic pseudopeptides (ACPPs) mixing α- and aza-β3 -amino acids were developed. Cyclopseudopeptide sequences were designed to investigate the impact of some intrinsic molecular parameters on their biological activities. Fine changes in the nature of the side chains strongly modulated the selectivity of the ACPPs with regard to hemolysis versus antimicrobial activity. The conformational preference of such compounds in various media was extensively studied, and the typical structure of cyclic α/aza-β3 -pseudopeptides is described for the first time. Interestingly, such scaffolds are stabilized by successive inverse γ- and N-N turns (hydrazino turns), a unique feature due to the aza-β3 residues. The α-amino acid side chains form a cluster on one face of the ring, while the aza-β3 -amino acid side chains are projected around the ring in the equatorial orientation. Such structural data are particularly valuable to fine-tune the bioactivity of these ACPPs by a structure-based approach.

Our teams recorded great results at the Montpellier marathon 2018!

Mens sana in corpore sano !

Two marathon relay teams from our group registered great times at this year edition of the Montpellier Marathon. Our senior team finished in just under 3 hours at the amazing 10th place out of 380 teams. Our youth team recorded a great result for their first participation and finished 88th for about 3h 50min. Congratulations to both teams for the participation and the achievments !