Structural highlights
Function
SPG1_STRSG Binds to the constant Fc region of IgG with high affinity.
Publication Abstract from PubMed
Strategic incorporation of achiral C(alpha,alpha)-dialkylated amino acids with bulky substituents into peptides can be used to promote extended strand conformations and inhibit protein-protein interactions associated with amyloid formation. In this work, we evaluate the thermodynamic impact of chiral C(alpha,alpha) monomers on folding preferences in such systems through introduction of a series of C(alpha)-methylated and C(alpha)-ethylated residues into a beta-hairpin host sequence. Depending on stereochemical configuration of the artificial monomer and potential for additional hydrophobic packing, a C(alpha)-ethyl-C(alpha)-propyl glycine residue can provide similar or enhanced folded stability relative to an achiral C(alpha,alpha)-diethyl analogue.
Effects of chirality and side chain length in C(alpha,alpha)-dialkylated residues on beta-hairpin peptide folded structure and stability.,Heath SL, Horne WS, Lengyel GA Org Biomol Chem. 2023 Aug 9;21(31):6320-6324. doi: 10.1039/d3ob00963g. PMID:37503895[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Heath SL, Horne WS, Lengyel GA. Effects of chirality and side chain length in C(α,α)-dialkylated residues on β-hairpin peptide folded structure and stability. Org Biomol Chem. 2023 Aug 9;21(31):6320-6324. PMID:37503895 doi:10.1039/d3ob00963g
