Congrats to Y. Wu, et al. for their paper accepted by Chemical Science

Peptides constrained through multiple disulfides (or disulfide-rich peptides, DRPs) have been an emerging frontier for ligand and drug discovery. Such peptides have the potential to combine the binding capability of biologics with the stability and bioavailability of smaller molecules. However, DRPs with stable three-dimensional (3D) structures are usually of natural origin or engineered f...

Congrats to S. Yao, et al. for their paper accepted by Nature Communications

Peptide heterodimers are prevalent in nature, which are not only functional macromolecules but molecular tools for chemical and synthetic biology. Computational methods have also been developed to design heterodimers of advanced functions. However, these peptide heterodimers are usually formed through noncovalent interactions, which are prone to dissociate and subject to concentration-depe...

Congrats to H. Dong, et al. for their paper accepted by Journal of the American Chemical Society

The engineering of naturally occurring disulfide-rich peptides (DRPs) has been significantly hampered by the difficulty of manipulating disulfide pairing. New DRPs that take advantage of fold-directing motifs and noncanonical thiol-bearing amino acids are easy-to-fold with expected disulfide connectivities, representing a new class of scaffolds for the development of peptide ligands and th...

Congrats to J. Zha, et al. for their paper accepted by Chemcal Science

Natural disulfide-rich peptides (DRPs) are valuable scaffolds for the development of new bioactive molecules and therapeutics. However, there are only a limited number of topologically distinct DRP folds in nature, and most of them suffer from the problem of in vitro oxidative folding. Thus, strategies to design DRPs with new constrained topologies beyond the scope of natural folds are desired....

Congrats to S. Lu & Y. Wu et.al for their paper accepted by J. Am. Chem. Soc.

​Disulfide-rich peptides (DRPs) have been an emerging frontier for drug discovery. There have been two DRPs approved as drugs (i.e., Ziconotide and Linaclotide), and many others are undergoing preclinical studies or in clinical trials. All of these DRPs are of nature origin or derived from natural peptides. It is still a challenge to design new DRPs without recourse to natural scaffolds due to...

Congrats to X. Zheng, et al. for their paper accepted by J. Am. Chem. Soc.

Disulfide-rich peptides are emerging as potential templates for drug design applications. However, the synthesis and reengineering of disulfide-rich peptides is challenging, owing to the complexity of...

J. Liu and J. Liang's work was accepted by Anal. Chem.

Peptides have been a promising molecular scaffold for the development of potential therapeutics with high affinity and specificity to biomacromolecules. However, their inherent proteolytic instability...

The collaboration work with Hiroaki Suga's group was accepted by Angew. Chem., Congratulations!

We developed thioether-bonded fluorescent probes that enable us to explore thiol-mediated thioether (and disulfide) exchange reactions on the cell surface through fluorescence recovery and/or cell ima...

W. Liu's work was accepted by Angew. Chem.. Congratulations!

In this work, we report the discovery of a small phenyl molecule with four isosteric thiolate-reactive groups of sequentially-varied reactivity, and how this molecule was exploited in combination with...