p-gp score calculated by an unpublished pfizer method (Pfizer Inc)
90
Structured Review
Pfizer Inc
p-gp score calculated by an unpublished pfizer method
P Gp Score Calculated By An Unpublished Pfizer Method, supplied by Pfizer Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/p-gp+score+calculated+by+an+unpublished+pfizer+method/p+gp+score+calculated+by+an+unpublished+pfizer+method/pm23006604-75-370-376
Average 90 stars, based on 1 article reviews
P Gp Score Calculated By An Unpublished Pfizer Method, supplied by Pfizer Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/p-gp+score+calculated+by+an+unpublished+pfizer+method/p+gp+score+calculated+by+an+unpublished+pfizer+method/pm23006604-75-370-376
Average 90 stars, based on 1 article reviews
p-gp score calculated by an unpublished pfizer method - by Bioz Stars,
2026-09
90/100 stars
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Membrane:Article Title: How hydrogen bonds impact P-glycoprotein transport and permeability. Article Snippet: H-bonding is known to be an important parameter for describing drug permeability34–36 H-bonding of the solute with water predominates over H-bonds involving polar atoms of the phospholipid head groups, which is consistent with the number of water molecules present in this membrane region exceeding the number of lipid molecules.37 However, the degree to which a compound interacts with the solvent water phase is not simply determined by the total number of H-bonds it is able to form with water molecules, but by the relative strength of these H-bonds.38 The size and nature of the non-polar portion of a molecule, which depend upon the conformation assumed in that region of the membrane, also has a significant influence on the strength of the H-bonds the molecule is able to form.37,38 During transmembrane diffusion, movement of the solute from the region of minimum free energy (at 15 Å from the bilayer center) into the ordered chain region within the bilayer interior is energetically disfavored and this is largely due to the progressive breakage of H-bonds.37 This concept of desolvation originally proposed by Stein39 was reintroduced by Burton’s laboratory in the early 1990s with the demonstration that passive diffusion of a congener series of purposefully designed, small neutral peptides correlated with the number of H-bond groups.40 As the number of solute-solvent H-bonds increased, permeability decreased and removal of the peptide bonds by N-methylation resulted in predictable increases in permeability.41,42 As described in the case of P-gp, and also true for permeability, consideration of the HBD/HBA strength would be critical when Table 1 Summary of potency and P-glycoprotein data for compound examples from Myatt et al.32 N N O N N R N N N N N O R R 1, 2 - 6 7 - 8 1 2 3 Compound R1 R2 R3 a2d1 IC50 (nM) Predicted P-gp scorea P-gp Efflux ratiob 1 N — — 2 0.38 1.4 2 N OH — — 32 0.40 9.1 3 N NH2 — — 2 0.68 29 4 N OH — — 5 0.36 9 5 N OMe — — 6 0.01 1.8 6 N OMe — — 5 0.03 1.8 7 — OCF3 Cl 8 NA Non-substrate 8 — F OEt 8 NA Non-substrate a Solvent:Article Title: How hydrogen bonds impact P-glycoprotein transport and permeability. Article Snippet: H-bonding is known to be an important parameter for describing drug permeability34–36 H-bonding of the solute with water predominates over H-bonds involving polar atoms of the phospholipid head groups, which is consistent with the number of water molecules present in this membrane region exceeding the number of lipid molecules.37 However, the degree to which a compound interacts with the solvent water phase is not simply determined by the total number of H-bonds it is able to form with water molecules, but by the relative strength of these H-bonds.38 The size and nature of the non-polar portion of a molecule, which depend upon the conformation assumed in that region of the membrane, also has a significant influence on the strength of the H-bonds the molecule is able to form.37,38 During transmembrane diffusion, movement of the solute from the region of minimum free energy (at 15 Å from the bilayer center) into the ordered chain region within the bilayer interior is energetically disfavored and this is largely due to the progressive breakage of H-bonds.37 This concept of desolvation originally proposed by Stein39 was reintroduced by Burton’s laboratory in the early 1990s with the demonstration that passive diffusion of a congener series of purposefully designed, small neutral peptides correlated with the number of H-bond groups.40 As the number of solute-solvent H-bonds increased, permeability decreased and removal of the peptide bonds by N-methylation resulted in predictable increases in permeability.41,42 As described in the case of P-gp, and also true for permeability, consideration of the HBD/HBA strength would be critical when Table 1 Summary of potency and P-glycoprotein data for compound examples from Myatt et al.32 N N O N N R N N N N N O R R 1, 2 - 6 7 - 8 1 2 3 Compound R1 R2 R3 a2d1 IC50 (nM) Predicted P-gp scorea P-gp Efflux ratiob 1 N — — 2 0.38 1.4 2 N OH — — 32 0.40 9.1 3 N NH2 — — 2 0.68 29 4 N OH — — 5 0.36 9 5 N OMe — — 6 0.01 1.8 6 N OMe — — 5 0.03 1.8 7 — OCF3 Cl 8 NA Non-substrate 8 — F OEt 8 NA Non-substrate a Diffusion-based Assay:Article Title: How hydrogen bonds impact P-glycoprotein transport and permeability. Article Snippet: H-bonding is known to be an important parameter for describing drug permeability34–36 H-bonding of the solute with water predominates over H-bonds involving polar atoms of the phospholipid head groups, which is consistent with the number of water molecules present in this membrane region exceeding the number of lipid molecules.37 However, the degree to which a compound interacts with the solvent water phase is not simply determined by the total number of H-bonds it is able to form with water molecules, but by the relative strength of these H-bonds.38 The size and nature of the non-polar portion of a molecule, which depend upon the conformation assumed in that region of the membrane, also has a significant influence on the strength of the H-bonds the molecule is able to form.37,38 During transmembrane diffusion, movement of the solute from the region of minimum free energy (at 15 Å from the bilayer center) into the ordered chain region within the bilayer interior is energetically disfavored and this is largely due to the progressive breakage of H-bonds.37 This concept of desolvation originally proposed by Stein39 was reintroduced by Burton’s laboratory in the early 1990s with the demonstration that passive diffusion of a congener series of purposefully designed, small neutral peptides correlated with the number of H-bond groups.40 As the number of solute-solvent H-bonds increased, permeability decreased and removal of the peptide bonds by N-methylation resulted in predictable increases in permeability.41,42 As described in the case of P-gp, and also true for permeability, consideration of the HBD/HBA strength would be critical when Table 1 Summary of potency and P-glycoprotein data for compound examples from Myatt et al.32 N N O N N R N N N N N O R R 1, 2 - 6 7 - 8 1 2 3 Compound R1 R2 R3 a2d1 IC50 (nM) Predicted P-gp scorea P-gp Efflux ratiob 1 N — — 2 0.38 1.4 2 N OH — — 32 0.40 9.1 3 N NH2 — — 2 0.68 29 4 N OH — — 5 0.36 9 5 N OMe — — 6 0.01 1.8 6 N OMe — — 5 0.03 1.8 7 — OCF3 Cl 8 NA Non-substrate 8 — F OEt 8 NA Non-substrate a Permeability:Article Title: How hydrogen bonds impact P-glycoprotein transport and permeability. Article Snippet: H-bonding is known to be an important parameter for describing drug permeability34–36 H-bonding of the solute with water predominates over H-bonds involving polar atoms of the phospholipid head groups, which is consistent with the number of water molecules present in this membrane region exceeding the number of lipid molecules.37 However, the degree to which a compound interacts with the solvent water phase is not simply determined by the total number of H-bonds it is able to form with water molecules, but by the relative strength of these H-bonds.38 The size and nature of the non-polar portion of a molecule, which depend upon the conformation assumed in that region of the membrane, also has a significant influence on the strength of the H-bonds the molecule is able to form.37,38 During transmembrane diffusion, movement of the solute from the region of minimum free energy (at 15 Å from the bilayer center) into the ordered chain region within the bilayer interior is energetically disfavored and this is largely due to the progressive breakage of H-bonds.37 This concept of desolvation originally proposed by Stein39 was reintroduced by Burton’s laboratory in the early 1990s with the demonstration that passive diffusion of a congener series of purposefully designed, small neutral peptides correlated with the number of H-bond groups.40 As the number of solute-solvent H-bonds increased, permeability decreased and removal of the peptide bonds by N-methylation resulted in predictable increases in permeability.41,42 As described in the case of P-gp, and also true for permeability, consideration of the HBD/HBA strength would be critical when Table 1 Summary of potency and P-glycoprotein data for compound examples from Myatt et al.32 N N O N N R N N N N N O R R 1, 2 - 6 7 - 8 1 2 3 Compound R1 R2 R3 a2d1 IC50 (nM) Predicted P-gp scorea P-gp Efflux ratiob 1 N — — 2 0.38 1.4 2 N OH — — 32 0.40 9.1 3 N NH2 — — 2 0.68 29 4 N OH — — 5 0.36 9 5 N OMe — — 6 0.01 1.8 6 N OMe — — 5 0.03 1.8 7 — OCF3 Cl 8 NA Non-substrate 8 — F OEt 8 NA Non-substrate a |