Structural Determinants of the Stability of Enzyme-Responsive Polyion Complex Nanoparticles Targeting Pseudomonas aeruginosa’s Elastase

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@article{c18824bbaef14e8993a439c8d94f6824,
title = "Structural Determinants of the Stability of Enzyme-Responsive Polyion Complex Nanoparticles Targeting Pseudomonas aeruginosa{\textquoteright}s Elastase",
abstract = "Here, we report how the stability of polyion complex (PIC) particles containing Pseudomonas aeruginosa{\textquoteright}s elastase (LasB) degradable peptides and antimicrobial poly(ethylene imine) is significantly improved by careful design of the peptide component. Three LasB‐degradable peptides are reported herein, all of them carrying the LasB‐degradable sequence −GLA− and for which the number of anionic amino acids and cysteine units per peptide were systematically varied. Our results suggest that while net charge and potential to cross‐link via disulfide bond formation do not have a predictable effect on the ability of LasB to degrade these peptides, a significant effect of these two parameters on particle preparation and stability is observed. A range of techniques has been used to characterize these new materials and demonstrates that increasing the charge and cross‐linking potential of the peptides results in PIC particles with better stability in physiological conditions and upon storage. These results highlight the importance of molecular design for the preparation of PIC particles and should underpin the future development of these materials for responsive drug delivery.",
author = "Ignacio Insua and Marion Petit and Blackman, {Lewis D.} and Robert Keogh and Ana{\"i}s Pitto-barry and O'reilly, {Rachel K.} and Peacock, {Anna F. A.} and Krachler, {Anne Marie} and Francisco Fernandez-trillo",
year = "2018",
month = apr,
day = "23",
doi = "10.1002/cnma.201800054",
language = "English",
journal = "ChemNanoMat",
issn = "2199-692X",
publisher = "Wiley",

}

RIS

TY - JOUR

T1 - Structural Determinants of the Stability of Enzyme-Responsive Polyion Complex Nanoparticles Targeting Pseudomonas aeruginosa’s Elastase

AU - Insua, Ignacio

AU - Petit, Marion

AU - Blackman, Lewis D.

AU - Keogh, Robert

AU - Pitto-barry, Anaïs

AU - O'reilly, Rachel K.

AU - Peacock, Anna F. A.

AU - Krachler, Anne Marie

AU - Fernandez-trillo, Francisco

PY - 2018/4/23

Y1 - 2018/4/23

N2 - Here, we report how the stability of polyion complex (PIC) particles containing Pseudomonas aeruginosa’s elastase (LasB) degradable peptides and antimicrobial poly(ethylene imine) is significantly improved by careful design of the peptide component. Three LasB‐degradable peptides are reported herein, all of them carrying the LasB‐degradable sequence −GLA− and for which the number of anionic amino acids and cysteine units per peptide were systematically varied. Our results suggest that while net charge and potential to cross‐link via disulfide bond formation do not have a predictable effect on the ability of LasB to degrade these peptides, a significant effect of these two parameters on particle preparation and stability is observed. A range of techniques has been used to characterize these new materials and demonstrates that increasing the charge and cross‐linking potential of the peptides results in PIC particles with better stability in physiological conditions and upon storage. These results highlight the importance of molecular design for the preparation of PIC particles and should underpin the future development of these materials for responsive drug delivery.

AB - Here, we report how the stability of polyion complex (PIC) particles containing Pseudomonas aeruginosa’s elastase (LasB) degradable peptides and antimicrobial poly(ethylene imine) is significantly improved by careful design of the peptide component. Three LasB‐degradable peptides are reported herein, all of them carrying the LasB‐degradable sequence −GLA− and for which the number of anionic amino acids and cysteine units per peptide were systematically varied. Our results suggest that while net charge and potential to cross‐link via disulfide bond formation do not have a predictable effect on the ability of LasB to degrade these peptides, a significant effect of these two parameters on particle preparation and stability is observed. A range of techniques has been used to characterize these new materials and demonstrates that increasing the charge and cross‐linking potential of the peptides results in PIC particles with better stability in physiological conditions and upon storage. These results highlight the importance of molecular design for the preparation of PIC particles and should underpin the future development of these materials for responsive drug delivery.

U2 - 10.1002/cnma.201800054

DO - 10.1002/cnma.201800054

M3 - Article

JO - ChemNanoMat

JF - ChemNanoMat

SN - 2199-692X

ER -