| |
|
|
|
|
|
|
|
|
1. |
Record Nr. |
UNINA9910484381203321 |
|
|
Autore |
Hu Kuan |
|
|
Titolo |
Development of in-tether carbon chiral center-induced helical peptide : methodology and applications / / Kuan Hu |
|
|
|
|
|
|
|
Pubbl/distr/stampa |
|
|
Singapore : , : Springer, , [2021] |
|
©2021 |
|
|
|
|
|
|
|
|
|
ISBN |
|
|
|
|
|
|
Edizione |
[1st ed. 2021.] |
|
|
|
|
|
Descrizione fisica |
|
1 online resource (XV, 102 p. 75 illus., 65 illus. in color.) |
|
|
|
|
|
|
Collana |
|
|
|
|
|
|
Disciplina |
|
|
|
|
|
|
Soggetti |
|
Peptides - Synthesis |
Cancer - Research |
Peptides - Biotechnology |
Chemistry Techniques, Synthetic |
Peptides - therapeutic use |
Peptides, Cyclic |
Biomedical Research |
|
|
|
|
|
|
|
|
Lingua di pubblicazione |
|
|
|
|
|
|
Formato |
Materiale a stampa |
|
|
|
|
|
Livello bibliografico |
Monografia |
|
|
|
|
|
Nota di contenuto |
|
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. |
|
|
|
|
|
|
|
|
Sommario/riassunto |
|
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. . |
|
|
|
|
|
| |