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• W1159702433 abstract "Antibody microarrays have the potential to revolutionize molecular detection in scientific, medical, and other biosensor applications, but their current use is limited because of poor reliability. It is hypothesized that one reason for their poor performance results from strong antibody-surface interactions that destabilize the antibody structure and create steric interference for antigen recognition. Using a recently developed coarse-grain protein-surface model that has been parameterized against experimental data, antibody-surface interactions for two antibody orientations on two types of surfaces have been investigated. The results show that regardless of attachment geometry, antibodies tend to collapse onto hydrophobic surfaces and exhibit lower overall stability compared to antibodies on hydrophilic surfaces or in bulk solution. The results provide an unprecedented view into the dynamics of antibodies on surfaces and offer new insights into the poor performance exhibited by current antibody microarrays." @default.
• W1159702433 created "2016-06-24" @default.
• W1159702433 creator A5035565477 @default.
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• W1159702433 date "2015-08-11" @default.
• W1159702433 modified "2023-09-27" @default.
• W1159702433 title "Communication: Antibody stability and behavior on surfaces" @default.
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• W1159702433 doi "https://doi.org/10.1063/1.4928455" @default.
• W1159702433 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26277119" @default.
• W1159702433 hasPublicationYear "2015" @default.
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