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Chemical and Physical Variability in Structural Isomers of an l/d ?-Sheet Peptide
Designed To Inhibit Amyloidogenesis
#MMPMID29202245
Maris NL
; Shea D
; Bleem A
; Bryers JD
; Daggett V
Biochemistry
2018[Feb]; 57
(5
): 507-510
PMID29202245
show ga
There has been much interest in synthetic peptides as inhibitors of aggregation
associated with amyloid diseases. Of particular interest are compounds that
target the cytotoxic soluble oligomers preceding the formation of mature,
nontoxic fibrils. This study explores physical and chemical differences between
two de novo-designed peptides that share an identical primary structure but
differ in backbone chirality at six key positions. We show that the presence of
alternating l/d-amino acid motifs dramatically increases aqueous solubility,
enforces ?-sheet secondary structure, and inhibits aggregation of the ?-amyloid
peptide implicated in Alzheimer's disease, in addition to neutralizing its
cytotoxicity. In contrast, the all-l-amino acid isomer does not form ?-sheet
structure and is insoluble and inactive.
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