Enzyme-responsive chiral self-sorting in amyloid-inspired minimalistic peptide amphiphiles

Abstract

Self-sorting is a spontaneous phenomenon that ensures formation of complex yet ordered multicomponent system and conceptualizes the design of artificial and orthogonally functional compartments. In the present study, we envisage...

Chirality Effects in Peptide Assembly Structures

“…Chiral selectivity is ubiquitous in nature, so it is expected that proteins and peptides tend to prefer homochiral molecular interactions. Studies of L - and D -stereoisomers of amyloid peptides, such as a 22-residue segment of β 2 -microglobulin and β-amyloid peptide (Aβ40), showed that amyloid fibril formation was stereospecific: L -enantiomer was deposited on L -seeds, and enantiomers did not cross-react with each other ( Esler et al, 1999 ; Wadai et al, 2005 ; Gupta et al, 2020 ). However, it has been demonstrated that mixing enantiomers can change the kinetics, morphology, and mechanical properties of peptide self-assemblies ( Nagy-Smith et al, 2017 ; McAulay et al, 2019 ; Bera et al, 2020 ; Qin et al, 2021 ).…”

Hierarchical self-assembly of aromatic peptide conjugates into supramolecular polymers: it takes two to tango

“…86,87 The properties of these materials depends on the length, composition, and sequence of peptides, 86 but is also strongly affected by the chirality of the amino acids and by the nature of the aromatic groups. [88][89][90][91][92][93][94][95][96] Such supramolecular self-assembly involves β-sheets formation and different type of arrangement are proposed: parallel, antiparallel or interlocked anti-parallel (Fig. 4).…”

Chiral Selectivity of Secondary Nucleation in Amyloid Fibril Propagation

“…If monomers of one enantiomer forms fibrils, it is typically observed that monomers of the other are unable to be incorporated into these mirror‐image seeds. Such enantioselective fibril growth has been established in a number of systems including β2‐microglobulin fragments, [30–32] amyloid β peptides, [31, 33, 34] and other short amyloidogenic peptides [28, 35, 36] . PolyQ peptides seem to be an exception to this rule [37] …”

“…Such enantioselective fibril growth has been established in a number of systems including β2‐microglobulin fragments,[ 30 , 31 , 32 ] amyloid β peptides,[ 31 , 33 , 34 ] and other short amyloidogenic peptides. [ 28 , 35 , 36 ] PolyQ peptides seem to be an exception to this rule. [37] …”