Abstract
Latex is a colloidal suspension derived from the Hevea brasiliensis tree, derived from natural rubber, poly(isoprene), and assorted constituents including proteins and phospholipids. These constituents are inherent to both natural rubber and latex serum. This investigation was undertaken to examine the impact of the deproteinization process on chemical and biological dynamics of natural rubber latex. Natural Rubber (NR) extracted from the pure latex (LNCP) was obtained through centrifugation, followed by six rounds of solvent purification (LP6). The structure was characterized using Fourier-transform infrared spectroscopy (FTIR), thermogravimetric analysis (TGA), differential scanning calorimetry (DSC), swelling test, surface zeta potential (ζ), scanning electron microscopy (SEM) and in vitro assay. The results revealed that the LP6 group presented decreased swelling kinetics, reduced cell adhesion and proliferation, and a smoother surface with decreased negative surface charge. Conversely, the LNCP group shown accelerated swelling, heightened adhesion and cellular growth, and a more negatively charged and rougher surface. As such, the attributes of latex serum and proteins have potential usage across numerous biomedical applications.
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