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      Biological Evaluation and 3D-QSAR Studies of Curcumin Analogues as Aldehyde Dehydrogenase 1 Inhibitors

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          Abstract

          Aldehyde dehydrogenase 1 (ALDH1) is reported as a biomarker for identifying some cancer stem cells, and down-regulation or inhibition of the enzyme can be effective in anti-drug resistance and a potent therapeutic for some tumours. In this paper, the inhibitory activity, mechanism mode, molecular docking and 3D-QSAR (three-dimensional quantitative structure activity relationship) of curcumin analogues (CAs) against ALDH1 were studied. Results demonstrated that curcumin and CAs possessed potent inhibitory activity against ALDH1, and the CAs compound with ortho di-hydroxyl groups showed the most potent inhibitory activity. This study indicates that CAs may represent a new class of ALDH1 inhibitor.

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          Role of aldehyde dehydrogenase in cyclophosphamide-resistant L1210 leukemia.

          Douglas Hilton (1984)
          A cyclophosphamide-resistant L1210 cell line has been shown to have unusually high aldehyde dehydrogenase activity. The sensitivity of this cell line to 4-methylcyclophosphamide and phosphoramide mustard in vivo and corresponding sensitivities in vitro indicate that 4-hydroxycyclophosphamide and/or aldophosphamide is the form in which cyclophosphamide reaches these tumor cells in mice and that intracellular aldehyde dehydrogenase activity is an important determinant of cyclophosphamide sensitivity in these leukemia cell lines.
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            Alpha-glucosidase inhibition of natural curcuminoids and curcumin analogs.

            Albert S C Chan, Lin Ma, Guang-Rong Liu … (2006)
            Natural curcumin (1), demethoxycurcumin (2) and bisdemethoxycurcumin (3) isolated from Curcuma longa (turmeric), and synthetic curcumin analogs (A(1-7), B(1-7), C(1-6) and D(1-7)) were evaluated in vitro for the alpha-glucosidase inhibitory activity via UV and circular dichroism (CD) spectroscopy. The results indicated that natural curcuminoid compound 3 showed a remarkable inhibitory effect with IC(50) of 23.0 microM, and the synthetic compounds A(2), B(2), C(2) and D(2) showed potent inhibitory effects with IC(50) of 2.8, 2.6, 1.6 and 8.2 microM, respectively. Kinetic study exhibited that the mechanism of alpha-glucosidase inhibition of both 3 and C(2) was non-competitive. The structure activity relationship revealed that the ortho dihydroxyl groups could form a more tight interaction with alpha-glucosidase to exert more potential inhibitory activities.
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              Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases.

              Matthew T Kitson, K Kitson-Wind, Malcolm Moore … (1998)
              . Enzymes of the aldehyde dehydrogenase family are required for the clearance of potentially toxic aldehydes, and are essential for the production of key metabolic regulators. The cytosolic, or class 1, aldehyde dehydrogenase (ALDH1) of higher vertebrates has an enhanced specificity for all-trans retinal, oxidising it to the powerful differentiation factor all-trans retinoic acid. Thus, ALDH1 is very likely to have a key role in vertebrate development. . The three-dimensional structure of sheep ALDH1 has been determined by X-ray crystallography to 2.35 A resolution. The overall tertiary and quaternary structures are very similar to those of bovine mitochondrial ALDH (ALDH2), but there are important differences in the entrance tunnel for the substrate. In the ALDH1 structure, the sidechain of the general base Glu268 is disordered and the NAD+ cofactor binds in two distinct modes. . The submicromolar Km of ALDH1 for all-trans retinal, and its 600-fold enhanced affinity for retinal compared to acetaldehyde, are explained by the size and shape of the substrate entrance tunnel in ALDH1. All-trans retinal fits into the active-site pocket of ALDH1, but not into the pocket of ALDH2. Two helices and one surface loop that line the tunnel are likely to have a key role in defining substrate specificity in the wider ALDH family. The relative sizes of the tunnels also suggest why the bulky alcohol aversive drug disulfiram reacts more rapidly with ALDH1 than ALDH2. The disorder of Glu268 and the observation that NAD+ binds in two distinct modes indicate that flexibility is a key facet of the enzyme reaction mechanism.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Mol Sci
                Journal ID (iso-abbrev): Int J Mol Sci
                Journal ID (publisher-id): ijms
                Title: International Journal of Molecular Sciences
                Publisher: Molecular Diversity Preservation International (MDPI)
                ISSN (Electronic): 1422-0067
                Publication date Collection: May 2014
                Publication date (Electronic): 16 May 2014
                Volume: 15
                Issue: 5
                Pages: 8795-8807
                Affiliations
                [1 ]School of Light Industry and Chemical Engineering, Guangdong University of Technology, Guangzhou 510500, China; E-Mails: wanghuibetty1988@ 123456126.com (H.W.); changyuanzhang@ 123456126.com (C.Z.); tzkcarlos@ 123456163.com (Z.T.); hxg_129@ 123456126.com (Y.H.); fumaihuanxue@ 123456126.com (Q.Z.); junzhao60@ 123456hotmail.com (J.Z.); zhengxi08@ 123456hotmail.com (X.Z.)
                [2 ]Guangzhou Improve Medical Technology Co., Ltd., Guangzhou 510530, China
                [3 ]Susan Lehman Cullman Laboratory for Cancer Research Ernest Mario School of Pharmacy, Rutgers, the State University of New Jersey, Piscataway, NJ 08854, USA
                Author notes
                [* ]Author to whom correspondence should be addressed; E-Mail: zhiyundu@ 123456gdut.edu.cn ; Tel.: +86-20-3932-2235; Fax: +86-20-3932-3363.
                Article
                Publisher ID: ijms-15-08795
                DOI: 10.3390/ijms15058795
                PMC ID: 4057759
                PubMed ID: 24840575
                SO-VID: 521cc8c8-db6f-4a2c-a278-19eae14c255e
                Copyright © © 2014 by the authors; licensee MDPI, Basel, Switzerland
                License:

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                Date received : 04 January 2014
                Date revision received : 13 March 2014
                Date accepted : 24 March 2014
                Categories
                Subject: Article

                ScienceOpen disciplines: Molecular biology
                Keywords: curcumin,curcumin analogues,aldh1,inhibitor,3d-qsar
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: curcumin, curcumin analogues, aldh1, inhibitor, 3d-qsar

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