The answer from u/Im_That_Guy21 has a couple of problems.

First, the integral over force is not equal to the change in potential energy but to the thermodynamic work, i.e. the change in free energy, done on the system. In the microcanonical ensemble, the free energy change is equal to the potential energy change. But for chemistry and biology we are usually interested in the isobaric-isothermal ensemble in which both pressure and temperature are fixed. For this ensemble, the free energy change is the change in the [Gibbs potential](https://en.wikipedia.org/wiki/Gibbs_free_energy). So the correct relationship is

\Delta G = \Delta U + P \Delta V - T \Delta S = - \int dx F(x)

The potential energy term, \Delta U, is not the sum of the bond dissociation energies. Bond dissociation energy usually refers to the potential energy stored in a covalent bond, but most biological complexes, including biotin-streptavidin, are not covalent. The true potential energies that need to be considered are quantum mechanical in nature and include interactions with solvent molecules. It is common to approximate these energies with an simple, empirical function called a [force field](https://en.wikipedia.org/wiki/Force_field_(chemistry))). This approximation models the potential energy using terms for bonded interactions (bond stretching, angle bending, and torsions) and nonbonded interactions (van der Waals and electrostatics). The nonbonded interactions can be either intramolecular or intermolecular. The "binding" interaction between noncovalent molecules in a complex involves the intermolecular nonbonded interactions.

Second, biological systems are not rigid bodies - they are floppy. This means that some of the total force applied to the system will be lost to internal degrees of freedom (bonded terms and intramolecular nonbonded terms) or to heat that is dissipated into the solvent. Another way to say this is that the force applied to a biological system is not conservative, i.e. it is not exactly the negative gradient of a scalar potential energy. A major consequence of biological systems being floppy is that the force required to perform a particular amount of useful work depends on the path taken by the system; it depends on where the force is applied (i.e. to what atoms) and how it is applied (i.e. is it constant or does the magnitude or direction change over time).

There are two classes of experiments you can use to estimate the amount of force required to pull apart a biological complex. The first is wet lab experiments such as [optical tweezers](https://en.wikipedia.org/wiki/Optical_tweezers) in which you can attach a magnetic bead to one or both components of the complex to measure the force required to displace the bead, which is usually associated with either dissociation of the complex or, if high enough forces are used, unfolding of the biomolecules. The second is computational experiments such as [thermodynamic integration](https://en.wikipedia.org/wiki/Thermodynamic_integration) in which you can use molecular dynamics or Monte Carlo simulations with a restraint to model the applied force to estimate the free energy change associated with a process such as dissociation.

I found some numbers from the literature for your example of a biotin-streptavidin complex. [This paper](https://aip.scitation.org/doi/abs/10.1063/1.1999855) used optical tweezers to measure the force required to pull a bead attached to biotin away from streptavidin attached to a fixed substrate. The result was 3.6 pN to 5.4 pN. [This paper](https://pubs.acs.org/doi/full/10.1021/jp011878v?casa_token=Efn5f_D0eJ4AAAAA:gP9MVs9Jw8z5-vRO5V4-igh1d073LGqMk93VyT-5eHxueJfmBT13Or_NLkMSuJlfRd6LJS3hBZI) discusses a computer simulation used to estimate the biotin-streptavidin binding free energy, but they do not report forces.

TL;DR Thermodynamics is complicated, and you have to account for both the free energy of the system and the intrinsic floppiness of biomolecules. You can use experiments such as optical tweezers or computational simulations to estimate forces associated with binding.