| Description |
1 online resource (xv, 102 pages) : illustrations (some color) |
| Series |
Springer theses : recognizing outstanding Ph. D. research, 2190-5053 |
|
Springer theses, 2190-5053
|
| Contents |
Introduction -- Synthesis of in-tether chiral center peptides and their biophysical properties study -- In-tether chiral center induced helical peptide modulators target p53-MDM2/MDMX and inhibit tumor growth in cancer stem cell -- Summary and conclusion |
| Summary |
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 |
| Notes |
"Doctoral thesis accepted by Peking University, Beijing, China." |
| Bibliography |
Includes bibliographical references |
| Notes |
Online resource; title from PDF title page (SpringerLink, viewed March 9, 2021) |
| Subject |
Peptides -- Biotechnology
|
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Peptides -- Synthesis.
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Cancer -- Research.
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Protein-protein interactions.
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Biochemical engineering.
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Biochemical engineering
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Cancer -- Research
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Peptides -- Biotechnology
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Peptides -- Synthesis
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Protein-protein interactions
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| Form |
Electronic book
|
| ISBN |
9789813366138 |
|
9813366133 |
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