Unknown

Dataset Information

0

Peptides and peptidomimetics as regulators of protein-protein interactions.


ABSTRACT: Protein-protein interactions are essential for almost all intracellular and extracellular biological processes. Regulation of protein-protein interactions is one strategy to regulate cell fate in a highly selective manner. Specifically, peptides are ideal candidates for inhibition of protein-protein interactions because they can mimic a protein surface to effectively compete for binding. Additionally, peptides are synthetically accessible and can be stabilized by chemical modifications. In this review, we survey screening and rational design methods for identifying peptides to inhibit protein-protein interactions, as well as methods for stabilizing peptides to effectively mimic protein surfaces. In addition, we discuss recent applications of peptides to regulate protein-protein interactions for both basic research and therapeutic purposes.

SUBMITTER: Cunningham AD 

PROVIDER: S-EPMC5496809 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Peptides and peptidomimetics as regulators of protein-protein interactions.

Cunningham Anna D AD   Qvit Nir N   Mochly-Rosen Daria D  

Current opinion in structural biology 20170104


Protein-protein interactions are essential for almost all intracellular and extracellular biological processes. Regulation of protein-protein interactions is one strategy to regulate cell fate in a highly selective manner. Specifically, peptides are ideal candidates for inhibition of protein-protein interactions because they can mimic a protein surface to effectively compete for binding. Additionally, peptides are synthetically accessible and can be stabilized by chemical modifications. In this  ...[more]

Similar Datasets

| S-EPMC6017787 | biostudies-literature
| S-EPMC4201125 | biostudies-literature
| S-EPMC8170677 | biostudies-literature
| S-EPMC4588174 | biostudies-literature
| S-EPMC8372203 | biostudies-literature
| S-EPMC6142068 | biostudies-literature
| S-EPMC6022873 | biostudies-literature
| S-EPMC8646791 | biostudies-literature
| S-EPMC8686049 | biostudies-literature
| S-EPMC1366589 | biostudies-literature