TY - JOUR
T1 - Spontaneous structural transition in phospholipid-inspired aromatic phosphopeptide nanostructures
AU - Pellach, Michal
AU - Atsmon-Raz, Yoav
AU - Simonovsky, Eyal
AU - Gottlieb, Hugo
AU - Jacoby, Guy
AU - Beck, Roy
AU - Adler-Abramovich, Lihi
AU - Miller, Yifat
AU - Gazit, Ehud
N1 - Publisher Copyright:
© 2015 American Chemical Society.
PY - 2015/4/28
Y1 - 2015/4/28
N2 - Phospholipid membranes could be considered a prime example of the ability of nature to produce complex yet ordered structures, by spontaneous and efficient self-assembly. Inspired by the unique properties and architecture of phospholipids, we designed simple amphiphilic decapeptides, intended to fold in the center of the peptide sequence, with a phosphorylated serine "head" located within a central turn segment, and two hydrophobic "tails". The molecular design also included the integration of the diphenylalanine motif, previously shown to facilitate self-assembly and increase nanostructure stability. Secondary structure analysis of the peptides indeed indicated the presence of stabilized conformations in solution, with a central turn connecting two hydrophobic "tails", and interactions between the hydrophobic strands. The mechanisms of assembly into supramolecular structures involved structural transitions between different morphologies, which occurred over several hours, leading to the formation of distinctive nanostructures, including half-elliptical nanosheets and curved tapes. The phosphopeptide building blocks appear to self-assemble via a particular combination of aromatic, hydrophobic and ionic interactions, as well as hydrogen bonding, as demonstrated by proposed constructed simulated models of the peptides and self-assembled nanostructures. Molecular dynamics simulations also gave insight into mechanisms of structural transitions of the nanostructures at a molecular level. Because of the biocompatibility of peptides, the phosphopeptide assemblies allow for expansion of the library of biomolecular nanostructures available for future design and application of biomedical devices.
AB - Phospholipid membranes could be considered a prime example of the ability of nature to produce complex yet ordered structures, by spontaneous and efficient self-assembly. Inspired by the unique properties and architecture of phospholipids, we designed simple amphiphilic decapeptides, intended to fold in the center of the peptide sequence, with a phosphorylated serine "head" located within a central turn segment, and two hydrophobic "tails". The molecular design also included the integration of the diphenylalanine motif, previously shown to facilitate self-assembly and increase nanostructure stability. Secondary structure analysis of the peptides indeed indicated the presence of stabilized conformations in solution, with a central turn connecting two hydrophobic "tails", and interactions between the hydrophobic strands. The mechanisms of assembly into supramolecular structures involved structural transitions between different morphologies, which occurred over several hours, leading to the formation of distinctive nanostructures, including half-elliptical nanosheets and curved tapes. The phosphopeptide building blocks appear to self-assemble via a particular combination of aromatic, hydrophobic and ionic interactions, as well as hydrogen bonding, as demonstrated by proposed constructed simulated models of the peptides and self-assembled nanostructures. Molecular dynamics simulations also gave insight into mechanisms of structural transitions of the nanostructures at a molecular level. Because of the biocompatibility of peptides, the phosphopeptide assemblies allow for expansion of the library of biomolecular nanostructures available for future design and application of biomedical devices.
KW - bioinspired design
KW - molecular dynamics simulation
KW - nanostructures
KW - peptides
KW - phosphorylation
KW - self-assembly
UR - http://www.scopus.com/inward/record.url?scp=84928974924&partnerID=8YFLogxK
U2 - 10.1021/acsnano.5b00133
DO - 10.1021/acsnano.5b00133
M3 - Article
C2 - 25802000
AN - SCOPUS:84928974924
SN - 1936-0851
VL - 9
SP - 4085
EP - 4095
JO - ACS Nano
JF - ACS Nano
IS - 4
ER -