TY - JOUR
T1 - Supramolecular Peptoid Structure Strengthens Complexation with Polyacrylic Acid Microgels
AU - Zhao, Wenhan
AU - Lin, Jennifer S.
AU - Nielsen, Josefine Eilsø
AU - Sørensen, Kristian
AU - Wadurkar, Anand Sunil
AU - Ji, Jingjing
AU - Barron, Annelise E.
AU - Nangia, Shikha
AU - Libera, Matthew R.
N1 - Publisher Copyright:
© 2024 American Chemical Society.
PY - 2024/2/12
Y1 - 2024/2/12
N2 - We have studied the complexation between cationic antimicrobials and polyanionic microgels to create self-defensive surfaces that responsively resist bacterial colonization. An essential property is the stable sequestration of the loaded (complexed) antimicrobial within the microgel under a physiological ionic strength. Here, we assess the complexation strength between poly(acrylic acid) [PAA] microgels and a series of cationic peptoids that display supramolecular structures ranging from an oligomeric monomer to a tetramer. We follow changes in loaded microgel diameter with increasing [Na+] as a measure of the counterion doping level. Consistent with prior findings on colistin/PAA complexation, we find that a monomeric peptoid is fully released at ionic strengths well below physiological conditions, despite its +5 charge. In contrast, progressively higher degrees of peptoid supramolecular structure display progressively greater resistance to salting out, which we attribute to the greater entropic stability associated with the complexation of multimeric peptoid bundles.
AB - We have studied the complexation between cationic antimicrobials and polyanionic microgels to create self-defensive surfaces that responsively resist bacterial colonization. An essential property is the stable sequestration of the loaded (complexed) antimicrobial within the microgel under a physiological ionic strength. Here, we assess the complexation strength between poly(acrylic acid) [PAA] microgels and a series of cationic peptoids that display supramolecular structures ranging from an oligomeric monomer to a tetramer. We follow changes in loaded microgel diameter with increasing [Na+] as a measure of the counterion doping level. Consistent with prior findings on colistin/PAA complexation, we find that a monomeric peptoid is fully released at ionic strengths well below physiological conditions, despite its +5 charge. In contrast, progressively higher degrees of peptoid supramolecular structure display progressively greater resistance to salting out, which we attribute to the greater entropic stability associated with the complexation of multimeric peptoid bundles.
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U2 - 10.1021/acs.biomac.3c01242
DO - 10.1021/acs.biomac.3c01242
M3 - Article
C2 - 38240722
AN - SCOPUS:85183498723
SN - 1525-7797
VL - 25
SP - 1274
EP - 1281
JO - Biomacromolecules
JF - Biomacromolecules
IS - 2
ER -