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Figure 2. Investigation of factors contributing to fast clearance of ACI-5891.1. (a) Human FcRn <t>(hFcRn)</t> binding of ACI-5891.1 at pH 6.0 (left panel) and pH 7.4 (right panel). SPR measurement performed using antibody concentrations of 3000 nM, 1000 nM, 333.3 nM, 111.0 nM, and 37.0 nM as depicted. Sensorgrams are shown in black lines. (b) Non-specific binding of ACI-5891.1 and ACI-5891.5 by heparin and insulin ELISA. Mean signals for both targets are reported as nonspecific binding score. (c) Surface representation of ACI-5891.1 Fv model colored according to Eisenberg’s scale of hydrophobicity (shown at the bottom of panel c). Intense red indicates the most hydrophobic residue while white represents the most hydrophilic residue.
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Figure 2. Investigation of factors contributing to fast clearance of ACI-5891.1. (a) Human FcRn <t>(hFcRn)</t> binding of ACI-5891.1 at pH 6.0 (left panel) and pH 7.4 (right panel). SPR measurement performed using antibody concentrations of 3000 nM, 1000 nM, 333.3 nM, 111.0 nM, and 37.0 nM as depicted. Sensorgrams are shown in black lines. (b) Non-specific binding of ACI-5891.1 and ACI-5891.5 by heparin and insulin ELISA. Mean signals for both targets are reported as nonspecific binding score. (c) Surface representation of ACI-5891.1 Fv model colored according to Eisenberg’s scale of hydrophobicity (shown at the bottom of panel c). Intense red indicates the most hydrophobic residue while white represents the most hydrophilic residue.
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Figure 2. Investigation of factors contributing to fast clearance of ACI-5891.1. (a) Human FcRn (hFcRn) binding of ACI-5891.1 at pH 6.0 (left panel) and pH 7.4 (right panel). SPR measurement performed using antibody concentrations of 3000 nM, 1000 nM, 333.3 nM, 111.0 nM, and 37.0 nM as depicted. Sensorgrams are shown in black lines. (b) Non-specific binding of ACI-5891.1 and ACI-5891.5 by heparin and insulin ELISA. Mean signals for both targets are reported as nonspecific binding score. (c) Surface representation of ACI-5891.1 Fv model colored according to Eisenberg’s scale of hydrophobicity (shown at the bottom of panel c). Intense red indicates the most hydrophobic residue while white represents the most hydrophilic residue.

Journal: mAbs

Article Title: Improved antibody pharmacokinetics by disruption of contiguous positive surface potential and charge reduction using alternate human framework.

doi: 10.1080/19420862.2023.2232087

Figure Lengend Snippet: Figure 2. Investigation of factors contributing to fast clearance of ACI-5891.1. (a) Human FcRn (hFcRn) binding of ACI-5891.1 at pH 6.0 (left panel) and pH 7.4 (right panel). SPR measurement performed using antibody concentrations of 3000 nM, 1000 nM, 333.3 nM, 111.0 nM, and 37.0 nM as depicted. Sensorgrams are shown in black lines. (b) Non-specific binding of ACI-5891.1 and ACI-5891.5 by heparin and insulin ELISA. Mean signals for both targets are reported as nonspecific binding score. (c) Surface representation of ACI-5891.1 Fv model colored according to Eisenberg’s scale of hydrophobicity (shown at the bottom of panel c). Intense red indicates the most hydrophobic residue while white represents the most hydrophilic residue.

Article Snippet: Biotinylated hFcRn (AcroBiosystems, cat # FCMH82W4) was immobilized on flow-cell 2 (fc2) of flowchannels 1 to 8 of a streptavidin (SA) sensor chip (Cytiva, cat# BR-1005-31) to reach a final surface density of approximatively 150 RU.

Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay, Residue