Biodynamers: self-organization-driven formation of doubly dynamic proteoids.
Polypeptide-type dynamic biopolymers (biodynamers) have been generated by polycondensation via acylhydrazone and imine formation of amino-acid-derived components that polymerize driven by self-organization. They have been characterized as globular particles, reminiscent of folded proteins, by cryo-TEM, LS, DOSY NMR, and SANS studies. The reversible polymers obtained show remarkably low dispersity and feature double covalent dynamics allowing for fine-tuning of both exchange and incorporation processes through pH control. In the course of build-up, they perform a selection of the most suitable building block, as indicated by the preferential incorporation of the more hydrophobic amino-acid component with increased rate and higher molecular weight of the polymer formed. The system described displays nucleation-elongation behavior driven by hydrophobic effects and represents a model for the operation of adaptation processes in the evolution of complex matter.
Institut de Science et d'Ingénierie Supramoléculaires (ISIS), Université de Strasbourg, 8, allée Gaspard Monge, 67000 Strasbourg, France.
Anna K H
AK
Hirsch
Eric
E
Buhler
Jean-Marie
JM
Lehn
D000596:Amino Acids / Q000737:chemistry; D001704:Biopolymers / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D015394:Molecular Structure; D008970:Molecular Weight; D010316:Particle Size; D013816:Thermodynamics
D000596:Amino Acids; D001704:Biopolymers