Design of a Peptide-Based Model Leads for Scavenging Anions.

ABSTRACT: Among several peptide-based anion recognition motifs, the "C^αNN" motif containing C_-1 ^α, N₀, and N₊₁ of three consecutive residues is unique in its mode of interaction. Having a spatial geometry of βαα or βαβ, this motif occurs in the N terminus of a helix and often found at the functional interface of a protein, mediating crucial biological significance upon interaction with anion(s). The interaction of anion(s) with chimeric peptide sequences containing the naturally occurring "C^αNN" motif (CPS224Ac, CPS226, and CPS228) reported in our previous attempts strongly confirms that the information regarding the interaction is embedded within the local sequences of the motif segment. At these prevailing circumstances, an effort h

SUBMITTER: Sheet T 

PROVIDER: S-EPMC7203709 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature