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Nano- and Micropatterned Polycaprolactone Cellulose Composite Surfaces with Tunable Protein Adsorption, Fibrin Clot Formation, and Endothelial Cellular Response.

ABSTRACT: This work describes the interaction of the human blood plasma proteins albumin, fibrinogen, and ?-globulins with micro- and nanopatterned polymer interfaces. Protein adsorption studies were correlated with the fibrin clotting time of human blood plasma and with the growth of primary human pulmonary artery endothelial cells (hECs) on these patterns. It was observed that blends of polycaprolactone (PCL) and trimethylsilyl-protected cellulose form various thin-film patterns during spin coating, depending on the mass ratio of the polymers in the spinning solutions. Vapor-phase acid-catalyzed deprotection preserves these patterns but yields interfaces that are composed of hydrophilic cellulose domains enclosed by hydrophobic PCL. The blood plasma proteins are repelled by the cellulose domains, allowing for a suggested selective protein deposition on the PCL domains. An inverse proportional correlation is observed between the amount of cellulose present in the films and the mass of irreversibly adsorbed proteins. This results in significantly increased fibrin clotting times and lower masses of deposited clots on cellulose-containing films as revealed by quartz crystal microbalance with dissipation measurements. Cell viability of hECs grown on these surfaces was directly correlated with higher protein adsorption and faster clot formation. The results show that presented patterned polymer composite surfaces allow for a controllable blood plasma protein coagulation and a significant biological response from hECs. It is proposed that this knowledge can be utilized in regenerative medicine, cell cultures, and artificial vascular grafts by a careful choice of polymers and patterns.

SUBMITTER: Mohan T

PROVIDER: S-EPMC6750646 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature

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Nano- and Micropatterned Polycaprolactone Cellulose Composite Surfaces with Tunable Protein Adsorption, Fibrin Clot Formation, and Endothelial Cellular Response.

Mohan Tamilselvan T Nagaraj Chandran C Nagy Bence M BM Bračič Matej M Maver Uroš U Olschewski Andrea A Stana Kleinschek Karin K Kargl Rupert R

Biomacromolecules 20190529 6

This work describes the interaction of the human blood plasma proteins albumin, fibrinogen, and γ-globulins with micro- and nanopatterned polymer interfaces. Protein adsorption studies were correlated with the fibrin clotting time of human blood plasma and with the growth of primary human pulmonary artery endothelial cells (hECs) on these patterns. It was observed that blends of polycaprolactone (PCL) and trimethylsilyl-protected cellulose form various thin-film patterns during spin coating, dep ...[more]

PMID: 31070898

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Project description:The adsorption of amyloidogenic peptides, amyloid beta 1-40 (A?1-40), alpha-synuclein (?-syn), and beta 2 microglobulin (?2m), was attempted over the surface of nano-gold colloidal particles, ranging from d = 10 to 100 nm in diameter (d). The spectroscopic inspection between pH 2 and pH 12 successfully extracted the critical pH point (pHo) at which the color change of the amyloidogenic peptide-coated nano-gold colloids occurred due to aggregation of the nano-gold colloids. The change in surface property caused by the degree of peptide coverage was hypothesized to reflect the ?pHo, which is the difference in pHo between bare gold colloids and peptide coated gold colloids. The coverage ratio (?) for all amyloidogenic peptides over gold colloid of different sizes was extracted by assuming ? = 0 at ?pHo = 0. Remarkably, ? was found to have a nano-gold colloidal size dependence, however, this nano-size dependence was not simply correlated with d. The geometric analysis and simulation of reproducing ? was conducted by assuming a prolate shape of all amyloidogenic peptides. The simulation concluded that a spiking-out orientation of a prolate was required in order to reproduce the extracted ?. The involvement of a secondary layer was suggested; this secondary layer was considered to be due to the networking of the peptides. An extracted average distance of networking between adjacent gold colloids supports the binding of peptides as if they are "entangled" and enclosed in an interfacial distance that was found to be approximately 2 nm. The complex nano-size dependence of ? was explained by available spacing between adjacent prolates. When the secondary layer was formed, A?1-40 and ?-syn possessed a higher affinity to a partially negative nano-gold colloidal surface. However, ?2m peptides tend to interact with each other. This difference was explained by the difference in partial charge distribution over a monomer. Both A?1-40 and ?-syn are considered to have a partial charge (especially ?+) distribution centering around the prolate axis. The ?2m, however, possesses a distorted charge distribution. For a lower ? (i.e., ? <0.5), a prolate was assumed to conduct a gyration motion, maintaining the spiking-out orientation to fill in the unoccupied space with a tilting angle ranging between 5° and 58° depending on the nano-scale and peptide coated to the gold colloid.

Dataset Information

Nano- and Micropatterned Polycaprolactone Cellulose Composite Surfaces with Tunable Protein Adsorption, Fibrin Clot Formation, and Endothelial Cellular Response.

Publications

Nano- and Micropatterned Polycaprolactone Cellulose Composite Surfaces with Tunable Protein Adsorption, Fibrin Clot Formation, and Endothelial Cellular Response.

Similar Datasets

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