4-Adamantyl-(2-(arylidene)hydrazinyl)thiazoles potential anti-diabetic agents: Experimental and docking studies - supplementary material

¹H NMR, ¹³C NMR and Mass spec data for 3a-3o

  

Figure S28. The amino acid residues of Human Serum Albumin involved in binding active site FA1 (top) and FA6/7 (bottom) with 3a are listed.

  

Figure S29. The amino acid residues of Human Serum Albumin involved in binding active site FA1 (top) and FA6/7 (bottom) with 3b are listed.

  

Figure S30. The amino acid residues of Human Serum Albumin involved in binding active site FA1 (top) and FA6/7 (bottom) with 3c are listed.

  

Figure S31. The amino acid residues of Human Serum Albumin involved in binding active site FA1 (top) and FA6/7 (bottom) with 3d are listed.

  

Figure S32. The amino acid residues of Human Serum Albumin involved in binding active site FA1 (top) and FA6/7 (bottom) with 3e are listed.

  

Figure S33. The amino acid residues of Human Serum Albumin involved in binding active site FA1 (top) and FA6/7 (bottom) with 3f are listed.

  

Figure S34. The amino acid residues of Human Serum Albumin involved in binding active site FA1 (top) and FA6/7 (bottom) with 3g are listed.

  

Figure S35. The amino acid residues of Human Serum Albumin involved in binding active site FA1 (top) and FA6/7 (bottom) with 3h are listed.

  

Figure S36. The amino acid residues of Human Serum Albumin involved in binding active site FA1 (top) and FA6/7 (bottom) with 3i are listed.

  

Figure S37. The amino acid residues of Human Serum Albumin involved in binding active site FA1 (top) and FA6/7 (bottom) with amino guanidine are listed.

  

Figure S38. The amino acid residues of Human Pancreatic Alpha Amylase involved in binding with 3a (top) 3b (center) and 3c (bottom).

  

Figure S39. The amino acid residues of Human Pancreatic Alpha Amylase involved in binding with 3d (top) 3e (center) and 3f (bottom).

  

Figure S40. The amino acid residues of Human Pancreatic Alpha Amylase involved in binding with 3g (top) 3h (center) and 3i (bottom).

  

Figure S41. The amino acid residues of Human Pancreatic Alpha Amylase involved in binding with 3j (top) 3k (center) and 3l (bottom).

  

Figure S42. The amino acid residues of Human Pancreatic Alpha Amylase involved in binding with 3m (top) 3n (center) and 3o (bottom).

 Figure S43. The amino acid residues of Human Pancreatic Alpha Amylase involved in binding with Acarbose.  

  

Figure S44: Suggested mass fragmentation pattern of 4-adamantyl-(2-(4-bromobenzylidene)hydrazinyl)thiazole (3c).

  

Table S1. In silico antiglycation activity of compounds (3a-i) with (FA1) binding site of human serum albumin.

  

Table S2. In silico antiglycation activity of compounds (3a-i) with (FA6/7) binding site of human serum albumin.

  

Table S3: In silico molecular docking study of compounds 3(a-o), and reference acarbose with active site of alpha-amylase protein (PDB: 4W93).