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Tuning Collagen Molecular Aggregation Behavior: Solvent Shielding in a Biphasic Polar System for Oxidized Sodium Alginate-Mediated Cross-Linking

Year: 2026
Type: article
Abstract: Precise regulation of collagen molecular aggregation behavior is essential for designing high-performance collagen-based biomaterials. This study presents an innovative approach to tune collagen molecular aggregation behavior using oxidized sodium alginate (OSA) as a crosslinker within a biphasic acetic acid/1-ethyl-3-methylimidazolium acetate solvent system. Such polar solvent environment effectively shielded electrostatic interactions between OSA and collagen, fabricating the formation of homogeneous crosslinked network. Successful integration of OSA into collagen while preserving its native triple-helix structure was confirmed through comprehensive characterization including FTIR, XRD, and SDS-PAGE. Fluorescence spectroscopy identified a critical aggregation concentration of 1.70 mg/mL in the AA/[EMIM][Ac] solvent system and revealed a [NH2]/[CHO] ratio-governed aggregation transition. Below the threshold ratio of 1:20, limited availability of OSA resulted in a low crosslinking density, leading to the formation of small-sized collagen aggregates. Beyond this threshold, abundant OSA provided a high density of aldehyde groups, driving extensive crosslinking and the formation of large-sized collagen aggregates. Finally, molecular docking simulations of the special binding interactions between collagen and OSA were conducted to validate the intrinsic viscosity, DLS, DSC and AFM findings. This work affords both fundamental insights and a practical methodology for enhancing the functional properties of collagen-based biomaterials through tailoring aggregation behavior.
DOI: 10.1021/acs.biomac.5c02605
Authors: Lingyu Hua, Fengxian Ju, Zihan Shen, Ying-Zhou Li, Tianduo Li, Jing Xu, Huan Yang
Language: English
Subfield: Biomaterials
Open Access status: green
OpenAlex ID: W7140229666
FWCI:
Cites: 52
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