Evaluation of sequence variability in HIV-1 gp41 C-peptide helix-grafted proteins.

ABSTRACT: Many therapeutically-relevant protein-protein interactions (PPIs) have been reported that feature a helix and helix-binding cleft at the interface. Given this, different approaches to disrupting such PPIs have been developed. While short peptides (<15 amino acids) typically do not fold into a stable helix, researchers have reported chemical approaches to constraining helix structure. However, these approaches rely on laborious, and often expensive, chemical synthesis and purification. Our premise is that protein-based solutions that stabilize a therapeutically-relevant helix offer a number of advantages. In contrast to chemically constrained helical peptides, or minimal/miniature proteins, which must be synthesized (at great expense and labor), a protein can be expressed in a cellular syst

SUBMITTER: Tennyson RL 

PROVIDER: S-EPMC6013034 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature