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PreprintCC BY-NC-NDbioRxiv

A General Mathematical Model of Symport Based on Conformational Transitions

  1. 1School of Biomedical Engineering, Southern Medical University, Guangzhou, Guangdong Province, P.R. China

Abstract

General mathematical modeling of symport faces two fundamental challenges: (i) a unified kinetic description independent of protein-specific structural details; and (ii) quantitative cross-scale mapping between microscopic conformational transitions and macroscopic physiological observables. Grounded in the fundamental physiological principle of cellular homeostasis, we propose a unifying hypothesis for symporter gating: symporters actively regulate intracellular concentrations of specific solutes within thermodynamically feasible bounds. Based on this hypothesis, we construct a universal mathematical model of symporters, employing a minimal conformational cycle as the topological scaffold and probabilistic transition rates to quantitatively describe conformational interconversion kinetics. Model simulations of experimental data from the SGLT, NaPi-II, NKCC, and NBC transporter families yield consistent fits. The resulting parameters not only reproduce experimentally observed transport behaviors---but also reveal underlying mechanistic principles of symporter function.

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BibTeX
@misc{wang2026general,
  title = {{A General Mathematical Model of Symport Based on Conformational Transitions}},
  author = {Q. Wang and F. Liang},
  howpublished = {bioRxiv},
  year = {2026},
  month = oct,
  doi = {10.64898/2026.10.15.759425},
  url = {https://www.biorxiv.org/content/10.64898/2026.10.15.759425v1},
  note = {CC BY-NC-ND},
}
RIS
TY  - UNPB
TI  - A General Mathematical Model of Symport Based on Conformational Transitions
AU  - Q. Wang
AU  - F. Liang
PY  - 2026
DA  - 2026/10/15
PB  - bioRxiv
DO  - 10.64898/2026.10.15.759425
UR  - https://www.biorxiv.org/content/10.64898/2026.10.15.759425v1
AB  - General mathematical modeling of symport faces two fundamental challenges: (i) a unified kinetic description independent of protein-specific structural details; and (ii) quantitative cross-scale mapping between microscopic conformational transitions and macroscopic physiological observables. Grounded in the fundamental physiological principle of cellular homeostasis, we propose a unifying hypothesis for symporter gating: symporters actively regulate intracellular concentrations of specific solutes within thermodynamically feasible bounds. Based on this hypothesis, we construct a universal mathematical model of symporters, employing a minimal conformational cycle as the topological scaffold and probabilistic transition rates to quantitatively describe conformational interconversion kinetics. Model simulations of experimental data from the SGLT, NaPi-II, NKCC, and NBC transporter families yield consistent fits. The resulting parameters not only reproduce experimentally observed transport behaviors---but also reveal underlying mechanistic principles of symporter function.
ER  -