New characteristic signatures from time-dependent static light scattering during polymer depolymerization, with application to proteoglycan subunit degradation

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Abstract

Models were developed for the time-dependent light scattering intensity for simply branched (“comb”) polymers undergoing one or more of three distinguishable degradation mechanisms: (a) stripping off the side chains, (b) randomly degrading off the side chains, and (c) randomly degrading the backbone. The model equations were applied to the analysis of different types of degradation of simply branched biopolymers—bovine nasal cartilage proteoglycan subunits (or “monomers”); NaOH stripped off the glycosaminoglycan (GAG) chains from the protein backbone [mechanism (a)], whereas hyaluronidase seemed to randomly cleave the GAG side chains [mechanism (b)], and HCl both stripped the GAG side chains and randomly cleaved the protein backbone [combined mechanisms (a) and (c)]. The reactions were followed with time-dependent multiangle, static light scattering. The time-resolved total scattering technique allowed degradation rate constants and percentage of material in the branched polymer backbone and side chains to be determined, in addition to the mechanisms involved. These new time-dependent light scattering profiles are added to the growing library of functions from which deductions can be made concerning polymer structure and associated degradation mechanisms and kinetics. These conclusions, drawn from time-dependent “batch” light scattering, are substantiated by preliminary size exclusion chromatography results and chemical binding assays for sulfated GAGs. © 1995 John Wiley & Sons, Inc.

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