Biography:
Dr. Xiaohong Tan earned his Bachelor’s and Master’s degrees from Sichuan University, China, and his Ph.D. from Nanyang Technological University, Singapore. Following his postdoctoral training at the Center for Nucleic Acids Science and Technology at Carnegie Mellon University, USA, he began his independent research career in the Chemistry Department at Bowling Green State University, USA. His expertise spans nucleic acid chemistry, peptide chemistry, and protein biochemistry, with a particular focus on designing aptamer- and peptide-based probes for precise protein recognition, enabling the study of protein-protein and protein-nucleic acid interactions. Dr. Tan serves as an Associate Editor for Frontiers in Molecular Biosciences: Molecular Recognition and is also a member of the Editorial Board for Scientific Reports. His recent research has been published in high-impact journals, including Journal of the American Chemical Society, Nature Communications, Theranostics, Organic Letters, Analytical Chemistry, and Chemical Communications etc.
Dual-Handed Recognition: Targeting a Single Protein with Two Chemical Ligands
Studying protein-protein interactions (PPIs) is crucial to understanding cellular processes, as proteins are the primary functional molecules within cells. Peptides and aptamers, which bridge the gap between antibodies and small molecules in terms of size and physical properties, play key roles in studying PPIs. Peptides are ideal ligands for recognizing proteins through hydrogen bonds, van der Waals forces, and ionic interactions. They can be chemically synthesized at low cost, have relatively low molecular weights, and exhibit enhanced tissue and cellular penetration. Aptamers, short single-stranded RNA or DNA molecules, can form unique spatial structures that enable them to tightly and specifically bind to a variety of targets. As an attractive alternative to antibodies, aptamers, particularly DNA-based ones, offer several advantages, such as long shelf life, low toxicity, low immunogenicity, cost-effective chemical synthesis, and the ability to tolerate diverse chemical modifications. In this talk, I will introduce bivalent protein-binding ligands, which consist of aptamers and/or peptides. These ligands are composed of two subunits, each capable of interacting with separate binding sites on a single protein, providing a new strategy for modulating PPIs and enhancing affinity, specificity and efficacy in target recognition.
