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  • 1.
    Shahzad, Danish
    et al.
    Quaid I Azam Univ, Dept Chem, Islamabad 45320, Pakistan.
    Saeed, Aamer
    Quaid I Azam Univ, Dept Chem, Islamabad 45320, Pakistan.
    Larik, Fayaz Ali
    Quaid I Azam Univ, Dept Chem, Islamabad 45320, Pakistan.
    Channar, Pervaiz Ali
    Quaid I Azam Univ, Dept Chem, Islamabad 45320, Pakistan.
    Abbas, Qamar
    Univ Sindh, Dept Physiol, Jamshoro 76080, Pakistan.
    Alajmi, Mohamed F.
    King Saud Univ, Dept Pharmacognosy, Coll Pharm, Riyadh 11451, Saudi Arabia.
    Arshad, M. Ifzan
    Quaid I Azam Univ, Dept Chem, Islamabad 45320, Pakistan.
    Erben, Mauricio F.
    UNLP, CONICET, CEQUINOR, Dept Quim,Fac Ciencias Exactas,CCT La Plata, Blvd 120 E-60 & 64 1465, RA-1900 La Plata, Argentina.
    Hassan, Mubashir
    Kongju Natl Univ, Coll Nat Sci, Dept Biol Sci, 56 Gongjudehak Ro, Gongju 32588, Chungnam, South Korea.
    Raza, Hussain
    Kongju Natl Univ, Coll Nat Sci, Dept Biol Sci, 56 Gongjudehak Ro, Gongju 32588, Chungnam, South Korea.
    Seo, Sung-Yum
    Kongju Natl Univ, Coll Nat Sci, Dept Biol Sci, 56 Gongjudehak Ro, Gongju 32588, Chungnam, South Korea.
    El-Seedi, Hesham
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Farmaceutiska fakulteten, Institutionen för läkemedelskemi, Farmakognosi.
    Novel C-2 Symmetric Molecules as -Glucosidase and -Amylase Inhibitors: Design, Synthesis, Kinetic Evaluation, Molecular Docking and Pharmacokinetics2019Ingår i: Molecules, ISSN 1420-3049, E-ISSN 1420-3049, Vol. 24, nr 8, artikel-id 1511Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    A series of symmetrical salicylaldehyde-bishydrazine azo molecules, 5a-5h, have been synthesized, characterized by H-1-NMR and C-13-NMR, and evaluated for their in vitro -glucosidase and -amylase inhibitory activities. All the synthesized compounds efficiently inhibited both enzymes. Compound 5g was the most potent derivative in the series, and powerfully inhibited both -glucosidase and -amylase. The IC50 of 5g against -glucosidase was 0.35917 +/- 0.0189 mu M (standard acarbose IC50 = 6.109 +/- 0.329 mu M), and the IC50 value of 5g against -amylase was 0.4379 +/- 0.0423 mu M (standard acarbose IC50 = 33.178 +/- 2.392 mu M). The Lineweaver-Burk plot indicated that compound 5g is a competitive inhibitor of -glucosidase. The binding interactions of the most active analogues were confirmed through molecular docking studies. Docking studies showed that 5g interacts with the residues Trp690, Asp548, Arg425, and Glu426, which form hydrogen bonds to 5g with distances of 2.05, 2.20, 2.10 and 2.18 angstrom, respectively. All compounds showed high mutagenic and tumorigenic behaviors, and only 5e showed irritant properties. In addition, all the derivatives showed good antioxidant activities. The pharmacokinetic evaluation also revealed promising results

  • 2.
    Ujan, Rabail
    et al.
    Univ Sindh, Dr MA Kazi Inst Chem, Jamshoro 76080, Pakistan.
    Saeed, Aamer
    Quaid I Azam Univ, Dept Chem, Islamabad 45320, Pakistan.
    Channar, Pervaiz Ali
    Quaid I Azam Univ, Dept Chem, Islamabad 45320, Pakistan.
    Larik, Fayaz Ali
    Quaid I Azam Univ, Dept Chem, Islamabad 45320, Pakistan.
    Abbas, Qamar
    Univ Sindh, Dept Physiol, Jamshoro 76080, Pakistan.
    Alajmi, Mohamed F.
    King Saud Univ, Dept Pharmacognosy, Coll Pharm, Riyadh 11451, Saudi Arabia.
    El-Seedi, Hesham
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Farmaceutiska fakulteten, Institutionen för läkemedelskemi, Farmakognosi.
    Rind, Mahboob Ali
    Univ Sindh, Dr MA Kazi Inst Chem, Jamshoro 76080, Pakistan.
    Hassan, Mubashir
    Kongju Natl Univ, Coll Nat Sci, Dept Biol Sci, Gongju 314701, Chungnam, South Korea.
    Raza, Hussain
    Kongju Natl Univ, Coll Nat Sci, Dept Biol Sci, Gongju 314701, Chungnam, South Korea.
    Seo, Sung-Yum
    Kongju Natl Univ, Coll Nat Sci, Dept Biol Sci, Gongju 314701, Chungnam, South Korea.
    Drug-1,3,4-Thiadiazole Conjugates as Novel Mixed-Type Inhibitors of Acetylcholinesterase: Synthesis, Molecular Docking, Pharmacokinetics, and ADMET Evaluation2019Ingår i: Molecules, ISSN 1420-3049, E-ISSN 1420-3049, Vol. 24, nr 5, artikel-id 860Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    A small library of new drug-1,3,4-thiazidazole hybrid compounds (3a-3i) was synthesized, characterized, and assessed for their acetyl cholinesterase enzyme (AChE) inhibitory and free radical scavenging activities. The newly synthesized derivatives showed promising activities against AChE, especially compound 3b (IC50 18.1 +/- 0.9 nM), which was the most promising molecule in the series, and was substantially more active than the reference drug (neostigmine methyl sulfate; IC50 2186.5 +/- 98.0 nM). Kinetic studies were performed to elucidate the mode of inhibition of the enzyme, and the compounds showed mixed-type mechanisms for inhibiting AChE. The Ki of 3b (0.0031 mu M) indicates that it can be very effective, even at low concentrations. Compounds 3a-3i all complied with Lipinski's Rule of Five, and showed high drug-likeness scores. The pharmacokinetic parameters revealed notable lead-like properties with insignificant liver and skin-penetrating effects. The structure-activity relationship (SAR) analysis indicated pi-pi interactions with key amino acid residues related to Tyr124, Trp286, and Tyr341.

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