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Harnessing Avidity: Quantifying the Entropic and Energetic Effects of Linker Length and Rigidity for Multivalent Binding of Antibodies to HIV-1

Authors
  • Einav, Tal1
  • Yazdi, Shahrzad2
  • Coey, Aaron3
  • Bjorkman, Pamela J.3
  • Phillips, Rob1, 3, 4
  • 1 Department of Physics, California Institute of Technology, Pasadena, CA 91125, USA
  • 2 Department of Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
  • 3 f Technology, Pasadena, CA 91125, USA
  • 4 Department of Applied Physics, California Institute of Technology, Pasadena, CA 91125, USA
Type
Published Article
Journal
Cell Systems
Publisher
Cell Press
Publication Date
Nov 27, 2019
Volume
9
Issue
5
Pages
466–474
Identifiers
DOI: 10.1016/j.cels.2019.09.007
PMID: 31668801
PMCID: PMC6892280
Source
PubMed Central
Keywords
License
Unknown

Abstract

Antibodies enhance their functional affinity by binding an antigen at multiple sites. Because HIV-1 contains few binding targets, the ability of antibodies to neutralize the virus is greatly decreased. Here, we develop a statistical-mechanical model that predicts the efficacy of synthetic antibodies composed of two Fabs joined together by DNA linkers of different lengths and flexibilities. This model predicts a synthetic antibody’s neutralization potency based on its linker composition, providing a framework to guide the design of future multivalent therapies.

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