Tuning physical properties of polyurethane hard segments through extender chain length variation and doping of pentaerythritol and their effect on in vitro protein adsorption

Author:

Wagh Shrish G.1,Sahani Mayur H.2,Soni Hemant P.1ORCID

Affiliation:

1. Department of Chemistry Faculty of Science, The Maharaja Sayajirao University of Baroda Vadodara Gujarat India

2. Dr. Vikram Sarabhai Institute of Cell & Molecular Biology, Faculty of Science The Maharaja Sayajirao University of Baroda Vadodara Gujarat India

Abstract

AbstractThis study explores the synthesis and characterization of polyurethanes (PUs) derived from hexamethylene diisocyanate (HDI) and 1,n‐alkane diols with varying chain lengths (n = 4, 6, and 10). Additionally, pentaerythritol (PE) is introduced as a dopant in PU6 at different weight percentages (25%, 50%, 75%, and 1:1%w/w). The research encompasses a comprehensive analysis of PU properties, including morphology, crystallinity, surface area, porosity, thermal behavior, rheological properties, and electrical conductivity. Of particular interest is the evaluation of protein adsorption capabilities employing bovine serum albumin (BSA) and fibrinogen proteins in in vitro tests. The study emphasizes the crucial role played by the chain length between isocyanate and diol groups and the nature and strength of hydrogen bonds among chains in shaping the polymer's properties, especially crystallinity and biocompatibility. Among the synthesized PUs, PU6 emerges as the top performer in terms of crystallinity and biocompatibility. Furthermore, the addition of PE is found to act as a plasticizer, reducing the glass transition temperature (Tg) from 75°C to 31°C. Electrochemical Impedance Spectroscopy shows that doping influences charge transfer processes, rendering the material semi‐conducting, as evidenced by decreased conductance when adding silver nanoparticles to PU6. Notably, protein adsorption studies reveal that undoped PU6 displays superior protein resistance compared to its doped counterpart, with fibrinogen exhibiting a higher adsorption affinity than BSA. The study discusses a plausible mechanism underlying protein adsorption.

Publisher

Wiley

Subject

Materials Chemistry,Polymers and Plastics,Surfaces, Coatings and Films,General Chemistry

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