High affinity restricts the localization and tumor penetration of single-chain fv antibody molecules.

By G. Adams, R. Schier, A. McCall, H. Simmons, E. Horak, R. Alpaugh, J. Marks, L. Weiner. Cancer Research, 2001

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The Therapeutic Potential of Nanobodies (2019, background): “showed that high affinity limits tumour penetration and intratumoural diffusion [23] (i.”
Investigating the impact of nanoparticle size on active and passive tumor targeting efficiency. (2014, background): “As a result, smallerparticlesmaybe forcedoutof the tumordue to high interstitial pressures.(30,31)”
Engineered Protease-resistant Antibodies with Selectable Cell-killing Functions* (2013, background): “Because of high interstitial tumor pressure, antibodies often concentrate in the perivascular regions (56) and at the invasive front of the tumor, presumably in close proximity to proteases (44).”
Arming antibodies: prospects and challenges for immunoconjugates (2005, background): “Lower molecular weight mAb fragments also demonstrate improved tumor penetration and more homogeneous tissue distribution compared with intact mAb”
RosettaAntibodyDesign (RAbD): A general framework for computational antibody design (2017, background): “addition to their numerous applications in biotechnology by private companies, government, and academia [1-7].”
Therapeutic antibodies: successes, limitations and hopes for the future (2009, unknown): “Whereas one might presume that tighter binding is always better, several studies have shown that very high affinities can be suboptimal for therapeutic antibodies that target solid tumours (Adams et al., 2001).”