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.

The chapters in this book explore the transcultural, multi-ethnic, and cross-regional contexts and connections between the Buddhavatamsaka-sutra, Mount Wutai and the veneration of Manjusri that contributed to the establishment and successive transformations of the cult centered on Mount Wutai - and reduplications elsewhere. The contributions reflect on the literature, architecture, iconography, medicine, society, philosophy and several other aspects of the Wutai cult and its significant influence across several Asian cultures, such as Chinese, Japanese, Tibetan, Mongolian and Korean. This book is a significant new contribution to the study of the Wutai cult, and will be a great resource for academics, researchers, and advanced students of Religion, Philosophy, History, Architecture, Literature and Art. The chapters in this book were originally published in the journal Studies in Chinese Religions.

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.