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      Cinnamic Acid and Its Derivatives Inhibit Fructose-Mediated Protein Glycation

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          Abstract

          Cinnamic acid and its derivatives have shown a variety of pharmacologic properties. However, little is known about the antiglycation properties of cinnamic acid and its derivatives. The present study sought to characterize the protein glycation inhibitory activity of cinnamic acid and its derivatives in a bovine serum albumin (BSA)/fructose system. The results demonstrated that cinnamic acid and its derivatives significantly inhibited the formation of advanced glycation end products (AGEs) by approximately 11.96–63.36% at a concentration of 1 mM. The strongest inhibitory activity against the formation of AGEs was shown by cinnamic acid. Furthermore, cinnamic acid and its derivatives reduced the level of fructosamine, the formation of N ɛ-(carboxymethyl) lysine (CML), and the level of amyloid cross β-structure. Cinnamic acid and its derivatives also prevented oxidative protein damages, including effects on protein carbonyl formation and thiol oxidation of BSA. Our findings may lead to the possibility of using cinnamic acid and its derivatives for preventing AGE-mediated diabetic complications.

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          Quantification of beta-sheet amyloid fibril structures with thioflavin T.

          William H. Levine (1998)
          Article 0 comments Cited 163 times – based on 0 reviews     Review now
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            Use of aminoguanidine (Pimagedine) to prevent the formation of advanced glycation endproducts.

            Paul Thornalley (2003)
            Aminoguanidine (AG) is a prototype therapeutic agent for the prevention of formation of advanced glycation endproducts. It reacts rapidly with alpha,beta-dicarbonyl compounds such as methylglyoxal, glyoxal, and 3-deoxyglucosone to prevent the formation of advanced glycation endproducts (AGEs). The adducts formed are substituted 3-amino-1,2,4-triazine derivatives. Inhibition of disease mechanisms, particularly vascular complications in experimental diabetes, by AG has provided evidence that accumulation of AGEs is a risk factor for disease progression. AG has other pharmacological activities, inhibition of nitric oxide synthase and semicarbazide-sensitive amine oxidase (SSAO), at pharmacological concentrations achieved in vivo for which controls are required in anti-glycation studies. AG is a highly reactive nucleophilic reagent that reacts with many biological molecules (pyridoxal phosphate, pyruvate, glucose, malondialdehyde, and others). Use of high concentrations of AG in vitro brings these reactions and related effects into play. It is unadvisable to use concentrations of AG in excess of 500 microM if selective prevention of AGE formation is desired. The peak plasma concentration of AG in clinical therapy was ca. 50 microM. Clinical trial of AG to prevent progression of diabetic nephropathy was terminated early due to safety concerns and apparent lack of efficacy. Pharmacological scavenging of alpha-oxoaldehydes or stimulation of host alpha-oxoaldehyde detoxification remains a worthy therapeutic strategy to prevent diabetic complications and other AGE-related disorders.
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              Conformational constraints for amyloid fibrillation: the importance of being unfolded.

              Vladimir Uversky, Anthony Fink (2004)
              Recent reports give strong support to the idea that amyloid fibril formation and the subsequent development of protein deposition diseases originate from conformational changes in corresponding amyloidogenic proteins. In this review, recent findings are surveyed to illustrate that protein fibrillogenesis requires a partially folded conformation. This amyloidogenic conformation is relatively unfolded, and shares many structural properties with the pre-molten globule state, a partially folded intermediate frequently observed in the early stages of protein folding and under some equilibrium conditions. The inherent flexibility of such an intermediate is essential in allowing the conformational rearrangements necessary to form the core cross-beta structure of the amyloid fibril.
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                Author and article information

                Journal
                Journal ID (nlm-ta): 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: 2012
                Publication date (Electronic): 08 February 2012
                Volume: 13
                Issue: 2
                Pages: 1778-1789
                Affiliations
                [1 ]The Medical Food Research and Development Center, Department of Nutrition and Dietetics , Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, Thailand
                [2 ]Research Group of Herbal Medicine for Prevention and Therapeutic of Metabolic diseases, Chulalongkorn University, Bangkok 10330, Thailand; E-Mails: Kradat_pup@ 123456hotmail.com (W.S); Jamaea_p@ 123456hotmail.com (A.M.); ampam10@ 123456hotmail.com (S.N.); Siritorn.y@ 123456chula.ac.th (S.Y.)
                [3 ]Program in Clinical Biochemistry and Molecular Medicine, Department of Clinical Chemistry, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, Thailand
                [4 ]Department of Pharmacology, Faculty of Veterinary Science, Chulalongkorn University, Bangkok 10330, Thailand
                Author notes
                [* ]Author to whom correspondence should be addressed; E-Mail: Sirichai.a@ 123456chula.ac.th ; Tel.: +66-2-218-1067; Fax: +66-2-218-1076.
                Article
                Publisher ID: ijms-13-01778
                DOI: 10.3390/ijms13021778
                PMC ID: 3291992
                PubMed ID: 22408423
                SO-VID: 33a881e5-76b1-4354-b120-e478bc6d8337
                Copyright © © 2012 by the authors; licensee Molecular Diversity Preservation International, 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 : 13 January 2012
                Date revision received : 22 January 2012
                Date accepted : 31 January 2012
                Categories
                Subject: Article

                ScienceOpen disciplines: Molecular biology
                Keywords: diabetic complications,fructose,cinnamic acid,glycation,advanced glycation end products
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: diabetic complications, fructose, cinnamic acid, glycation, advanced glycation end products

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