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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

<strong>Figure S42. </strong>The amino acid residues of Human Pancreatic Alpha Amylase involved in binding with <strong>3m</strong> (top) <strong>3n</strong> (center) and <strong>3o</strong> (bottom).
 <strong>Figure S43. </strong>The amino acid residues of Human Pancreatic Alpha Amylase involved in binding with Acarbose.  

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

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

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

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