This Ph.D. thesis is composed by three chapters based on different interests in chemical biology. The first chapter describes my work on the chemical glycosylation of proteins by cell compatible biorthogonal ligation. Current existing methods for the chemical glycosylation of proteins are powerful, however they are limited for purified proteins. Also, multiple synthetic steps are required to functionalize glycans of interest. The author has developed new synthetic methods to functionalize a series of native bioactive oligosaccharides in 1-2 steps. These neo glycans have enabled the glycosylation of proteins and other biomolecules in the ways that are applicable in live cells, which are tetrazine-strain alkene/alkyne cycloaddition and chelation assisted CuAAC. The second chapter describes my work on inhibition of multivalent interactions between glycans and pathogenic bacterial lectin. While multivalent interactions have been successfully blocked by glycopolymer and glycodendrimer approaches, a structurally well-designed ligand is required to enhance the potency and selectivity. A PNA encoded heteroglycan library was investigated to discover various sets of divalent glycan inhibitors for corresponding pathogenic lectins and DNA display showed structural information of ligands for preferential lectins. Furthermore, the interaction was also inhibited by PNA-programed dynamic glycan assembly. The dynamic glycan assembly was stabilized only when multivalent lectin is exists and showed nanomolar affinity to pathogenic lectin BambL. The assembly also successfully blocked the invasion of BambL to human lung epithelial cell H1299 in 723 fold effectively compared with monomeric glycan. 6 The third chapter describes my work on the development of constrained peptide catalysts folded through PNA hybridization. Folded short peptide catalysts have great potential to imitate enzyme active site and perform enzyme-like functions and ground breaking peptide catalysts have been reported to perform the diverse stereo and regio selective reactions with rate acceleration. The 1,000 member folded peptide-PNA library was screened to observe enhanced catalytic activity for phosphate bond hydrolysis. Identified sequence had >25 fold increased activity when the peptide structure was folded through PNA hybridization and the activity was moderated by strand displacement. Furthermore, to apply this concept for more broad chemistry, metallo peptide-PNA catalyst was designed and synthesized to hydrolyse metal chelating ester.