Substitution at the C-3 position of catechins has an influence on the binding affinities against serum albumin

Physics & Astronomy

• albumins 97%
• serums 94%
• affinity 86%
• gallates 67%
• substitutes 62%
• quenching 45%
• tryptophan 45%
• drugs 33%
• esters 12%
• blue shift 11%
• red shift 11%
• fluorescence 8%
• carbon 7%
• wavelengths 5%
• simulation 4%

Chemical Compounds

• Catechin 92%
• Kd 59%
• Gallate 56%
• Substitution Reaction 49%
• (-)-Epigallocatechin 42%
• Tryptophan Residue 35%
• Gallate Ester 28%
• Warfarin 21%
• Molecular Surface 19%
• Acyl Group 18%
• Tryptophan 14%
• Blue 11%
• Wavelength 11%
• Red 10%
• Simulation 9%
• Length 9%
• Fluorescence 9%
• Carbon Atom 7%

Medicine & Life Sciences

• Catechin 100%
• Serum Albumin 80%
• epigallocatechin gallate 50%
• Human Serum Albumin 46%
• Bovine Serum Albumin 44%
• Tryptophan 41%
• Binding Sites 30%
• Drug Residues 21%
• Warfarin 13%
• Esters 13%
• Carbon 12%
• Pharmaceutical Preparations 10%
• Fluorescence 10%