Development of in tether carbon chiral center induced helical peptide : methodology and applications This book focuses on the development of stapled peptides a novel molecular modality used to regulate aberrant intracellular protein–protein interactions (PPIs). The author designs and presents a novel helical peptide stabilization methodology by constructing a chiral cross linker moiety namely “chiral center induced peptide helicity (CIH)”. The book demonstrates that a precisely positioned carbon chiral center on tether can decisively determine the secondary structure of a peptide and that the R configured peptide is helical while the S configured peptide is non helical. Further it reports that helicity enhanced R isomer peptides displayed significantly enhanced cell permeability and target binding affinity as well as tumor inhibition efficiency in comparison to S isomer peptides. The book will not only advance readers’ understanding of the basic principle of stapled peptides but also accelerate the clinical transformation of stapled peptide drugs. . Introduction Method to construct in tether chiral center constrained helical peptide Application in disrupting p53 MDM2 protein protein interactions Fabrication of nanomaterials with in tether chiral center constrained helical peptide.