Avidity and surface mobility in multivalent ligand–receptor binding
Source abstract
Abstract
Targeted drug delivery relies on two physical processes: the selective binding of a therapeutic particle to receptors on a specific cell membrane, followed by transport of the particle across the membrane. In this article, we address some of the challenges in controlling the thermodynamics and dynamics of these two processes by combining a simple experimental system with a statistical mechanical model. Specifically, we characterize and model multivalent ligand-receptor binding between colloidal particles and fluid lipid bilayers, as well as the surface mobility of membrane-bound particles. We show that the mobility of the receptors within the fluid membrane is key to both the thermodynamics and dynamics of binding. First, we find that the particle-membrane binding free energy-or avidity-is a strongly nonlinear function of the ligand-receptor affinity. We attribute the nonlinearity to a combination of multivalency and recruitment of fluid receptors to the binding site. Our results also suggest that partial wrapping of the bound particles by the membrane enhances avidity further. Second, we demonstrate that the lateral mobility of membrane-bound particles is also strongly influenced by the recruitment of receptors. Specifically, we find that the lateral diffusion coefficient of a membrane-bound particle is dominated by the hydrodynamic drag against the aggregate of receptors within the membrane. These results provide one of the first direct validations of the working theoretical framework for multivalent interactions. They also highlight that the fluidity and elasticity of the membrane are as important as the ligand-receptor affinity in determining the binding and transport of small particles attached to membranes.
Source: openalex_inverted_index · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Lipid Membrane Structure and Behavior · Surfactants and Colloidal Systems · Electrostatics and Colloid Interactions
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Martin A. Fisher School of Physics, Brandeis University, Waltham, MA 02453, USA
Brandeis Materials Research Science and Engineering Center, Brandeis University, Waltham, MA 02453, USA
Funding
Division of Materials Research · National Institute of General Medical Sciences · Richard and Susan Smith Family Foundation
References (57)
Show source-provided references
1. Bae · J. Controlled Release · 2011 · 153 · 19810.1016/j.jconrel.2011.06.001 ↗
2. Torchilin · Nat. Rev. Drug Discovery · 2014 · 13 · 81310.1038/nrd4333 ↗
3. Veiseh · Adv. Drug Delivery Rev. · 2010 · 62 · 28410.1016/j.addr.2009.11.002 ↗
4. Wilhelm · Nat. Rev. Mater. · 2016 · 1 · 1601410.1038/natrevmats.2016.14 ↗
5. Mishra · Nanomedicine · 2010 · 6 · 910.1016/j.nano.2009.04.008 ↗
6. B.Alberts , A. D.Johnson , J.Lewis , D.Morgan , M.Raff , K.Roberts and P.Walter , Molecular Biology of the Cell , Garland Science , New York, NY , 6th edn, 2015
7. Martinez-Veracoechea · Proc. Natl. Acad. Sci. U. S. A. · 2011 · 108 · 1096310.1073/pnas.1105351108 ↗
8. Curk · Proc. Natl. Acad. Sci. U. S. A. · 2017 · 114 · 721010.1073/pnas.1704226114 ↗
9. Carlson · ACS Chem. Biol. · 2007 · 2 · 11910.1021/cb6003788 ↗
10. Mammen · Angew. Chem., Int. Ed. · 1998 · 37 · 275410.1002/(SICI)1521-3773(19981102)37:20<2754::AID-ANIE2754>3.0.CO;2-3 ↗
11. Varilly · J. Chem. Phys. · 2012 · 137 · 09410810.1063/1.4748100 ↗
12. Angioletti-Uberti · Phys. Chem. Chem. Phys. · 2016 · 18 · 637310.1039/C5CP06981E ↗
13. Angioletti-Uberti · Phys. Rev. Lett. · 2014 · 113 · 12830310.1103/PhysRevLett.113.128303 ↗
14. Shimobayashi · Phys. Chem. Chem. Phys. · 2015 · 17 · 1561510.1039/C5CP01340B ↗
15. Di Michele · Phys. Rev. E · 2018 · 98 · 03240610.1103/PhysRevE.98.032406 ↗
16. Mognetti · Rep. Prog. Phys. · 2019 · 82 · 11660110.1088/1361-6633/ab37ca ↗
17. Block · Nano Lett. · 2016 · 16 · 438210.1021/acs.nanolett.6b01511 ↗
18. Parolini · Nat. Commun. · 2015 · 6 · 594810.1038/ncomms6948 ↗
19. Bachmann · Soft Matter · 2016 · 12 · 780410.1039/C6SM01515H ↗
20. Lanfranco · Langmuir · 2019 · 35 · 200210.1021/acs.langmuir.8b02707 ↗
21. Scheepers · Proc. Natl. Acad. Sci. U. S. A. · 2020 · 117 · 2269010.1073/pnas.2003968117 ↗
22. Liu · Nat. Commun. · 2020 · 11 · 483610.1038/s41467-020-18603-5 ↗
23. Deserno · Phys. Rev. E · 2004 · 69 · 03190310.1103/PhysRevE.69.031903 ↗
24. Koltover · Phys. Rev. Lett. · 1999 · 82 · 199110.1103/PhysRevLett.82.1991 ↗
25. Reynwar · Nature · 2007 · 447 · 46110.1038/nature05840 ↗
26. Sarfati · Phys. Rev. E · 2016 · 94 · 01260410.1103/PhysRevE.94.012604 ↗
27. van der Wel · Sci. Rep. · 2016 · 6 · 3282510.1038/srep32825 ↗
28. Šarić · Soft Matter · 2013 · 9 · 667710.1039/c3sm50188d ↗
29. Zuraw-Weston · Nanoscale · 2019 · 11 · 1846410.1039/C9NR06570A ↗
30. Wang · Nat. Commun. · 2015 · 6 · 725310.1038/ncomms8253 ↗
31. Prieve · Adv. Colloid Interface Sci. · 1999 · 82 · 9310.1016/S0001-8686(99)00012-3 ↗
32. Crocker · J. Colloid Interface Sci. · 1996 · 179 · 29810.1006/jcis.1996.0217 ↗
33. Volpe · Opt. Express · 2009 · 17 · 2397510.1364/OE.17.023975 ↗
34. Rogers · Proc. Natl. Acad. Sci. U. S. A. · 2011 · 108 · 1568710.1073/pnas.1109853108 ↗
35. Ben-Tal · Biophys. J. · 2000 · 79 · 118010.1016/S0006-3495(00)76372-7 ↗
36. Hagan · J. Chem. Phys. · 2009 · 130 · 11490210.1063/1.3086041 ↗
37. SantaLucia Jr. · Proc. Natl. Acad. Sci. U. S. A. · 1998 · 95 · 146010.1073/pnas.95.4.1460 ↗
38. Gumí-Audenis · Nanoscale · 2018 · 10 · 1476310.1039/C8NR03249A ↗
39. Marsh · Biochim. Biophys. Acta, Biomembr. · 2003 · 1615 · 3310.1016/S0005-2736(03)00197-4 ↗
40. Brenner · Chem. Eng. Sci. · 1961 · 16 · 24210.1016/0009-2509(61)80035-3 ↗
41. Evans · J. Fluid Mech. · 1988 · 194 · 55310.1017/S0022112088003106 ↗
42. P. J.Flory , Principles of Polymer Chemistry , Cornell University Press , Ithaca, NY , 1953
43. Kucik · Biophys. J. · 1999 · 76 · 31410.1016/S0006-3495(99)77198-5 ↗
44. Knight · Biophys. J. · 2010 · 99 · 287910.1016/j.bpj.2010.08.046 ↗
45. Saffman · Proc. Natl. Acad. Sci. U. S. A. · 1975 · 72 · 311110.1073/pnas.72.8.3111 ↗
46. Oppenheimer · Biophys. J. · 2009 · 96 · 304110.1016/j.bpj.2009.01.020 ↗
47. Hughes · J. Fluid Mech. · 1981 · 110 · 34910.1017/S0022112081000785 ↗
48. Petrov · Biophys. J. · 2008 · 94 · L4110.1529/biophysj.107.126565 ↗
49. Bunge · J. Phys. Chem. B · 2009 · 113 · 1642510.1021/jp9067747 ↗
50. Lopez · Langmuir · 2018 · 34 · 1500010.1021/acs.langmuir.8b01368 ↗
51. Helfrich · Z. Naturforsch. C · 1973 · 28 · 69310.1515/znc-1973-11-1209 ↗
52. McMahon · Nature · 2005 · 438 · 59010.1038/nature04396 ↗
53. Frost · Cell · 2008 · 132 · 80710.1016/j.cell.2007.12.041 ↗
54. Saranathan · Proc. Natl. Acad. Sci. U. S. A. · 2010 · 107 · 1167610.1073/pnas.0909616107 ↗
55. Sacanna · Soft Matter · 2011 · 7 · 163110.1039/C0SM01125H ↗
56. Markham · Nucleic Acids Res. · 2005 · 33 · W57710.1093/nar/gki591 ↗
57. N. R.Markham and M.Zuker , in UNAFold: Software for Nucleic Acid Folding and Hybridization , ed. J. M. Keith , Humana Press , Totowa, NJ , 2008 , pp. 3–31