Premium
Peptide‐Assisted Design of Precision Polymer Sequences: On the Relevance of the Side‐Chain Sequences and the Variability of the Backbone
Author(s) -
Celasun Sensu,
Maron Eva,
Börner Hans G.
Publication year - 2020
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.201900244
Subject(s) - peptide , side chain , chemistry , peptidomimetic , sequence (biology) , monomer , polymer , peptide sequence , combinatorial chemistry , dispersity , stereochemistry , polymer chemistry , organic chemistry , biochemistry , gene
Abstract Functional sequences of monodisperse, sequence‐defined oligo(amide‐urethane)s are designed based on a peptide sequence as blueprint. The translation of a discrete side‐chain functionality sequence from a known peptide‐based solubilizer of the photosensitizer meta ‐tetra(hydroxyphenyl)‐chlorin, into a non‐peptidic precision polymer backbone is demonstrated. The resulting peptidomimetic precision polymers retain the functions of the parent peptide sequence, showing analogues sensitivity toward single monomer mutations/exchanges and even exceeding the parent peptide equivalent by reaching up to 69% higher payload capacities and more favored release kinetics.