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      • Record: found
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      Heterocycles in Peptidomimetics and Pseudopeptides: Design and Synthesis †

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          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          This minireview provides a brief outline of the peculiar aspects of the preparation of peptidomimetic and pseudopeptidic structures containing heterocycles. In particular novel tricyclic structures are investigated as potential drugs.

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          Most cited references55

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          Translating cell biology into therapeutic advances in Alzheimer's disease.

          D. Selkoe (1999)
          Studies of the molecular basis of Alzheimer's disease exemplify the increasingly blurred distinction between basic and applied biomedical research. The four genes so far implicated in familial Alzheimer's disease have each been shown to elevate brain levels of the self-aggregating amyloid-beta protein, leading gradually to profound neuronal and glial alteration, synaptic loss and dementia. Progress in understanding this cascade has helped to identify specific therapeutic targets and provides a model for elucidating other neurodegenerative disorders.
          Article 0 comments Cited 197 times – based on 0 reviews     Review now
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            Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein.

            X Lin, Jordan Tang, Ali Dashti … (2000)
            The cDNAs of two new human membrane-associated aspartic proteases, memapsin 1 and memapsin 2, have been cloned and sequenced. The deduced amino acid sequences show that each contains the typical pre, pro, and aspartic protease regions, but each also has a C-terminal extension of over 80 residues, which includes a single transmembrane domain and a C-terminal cytosolic domain. Memapsin 2 mRNA is abundant in human brain. The protease domain of memapsin 2 cDNA was expressed in Escherichia coli and was purified. Recombinant memapsin 2 specifically hydrolyzed peptides derived from the beta-secretase site of both the wild-type and Swedish mutant beta-amyloid precursor protein (APP) with over 60-fold increase of catalytic efficiency for the latter. Expression of APP and memapsin 2 in HeLa cells showed that memapsin 2 cleaved the beta-secretase site of APP intracellularly. These and other results suggest that memapsin 2 fits all of the criteria of beta-secretase, which catalyzes the rate-limiting step of the in vivo production of the beta-amyloid (Abeta) peptide leading to the progression of Alzheimer's disease. Recombinant memapsin 2 also cleaved a peptide derived from the processing site of presenilin 1, albeit with poor kinetic efficiency. Alignment of cleavage site sequences of peptides indicates that the specificity of memapsin 2 resides mainly at the S(1)' subsite, which prefers small side chains such as Ala, Ser, and Asp.
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              Proteases universally recognize beta strands in their active sites.

              Joel Tyndall, W D Fairlie, B T Nall (2005)
              Article 0 comments Cited 62 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Pharmaceuticals (Basel)
                Journal ID (iso-abbrev): Pharmaceuticals (Basel)
                Journal ID (publisher-id): pharmaceuticals
                Title: Pharmaceuticals
                Publisher: MDPI
                ISSN (Electronic): 1424-8247
                Publication date (Electronic): 08 March 2012
                Publication date Collection: March 2012
                Volume: 5
                Issue: 3
                Pages: 297-316
                Affiliations
                Dipartimento di Chimica “Antonio Mario Tamburro”, Università degli Studi della Basilicata, Via Ateneo Lucano 10, Potenza 85100, Italy; Email: iole.cerminara@ 123456gmail.com (I.C.); lucia.chiummiento@ 123456unibas.it (L.C.); ambra.guarnaccio@ 123456gmail.com (A.G.); paolo.lupattelli@ 123456unibas.it (P.L.)
                Author notes
                [†]

                Dedicated to Professor Piero Spagnolo on the occasion of his 70th birthday.

                [* ] Author to whom correspondence should be addressed; Email: maria.funicello@ 123456unibas.it ; Tel.: +39-097-120-5490; Fax: +39-097-120-5678.
                Article
                Publisher ID: pharmaceuticals-05-00297
                DOI: 10.3390/ph5030297
                PMC ID: 3763636
                SO-VID: 7bcd93a5-79aa-4730-8a17-d295b2695ce6
                Copyright © © 2012 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 : 27 December 2011
                Date revision received : 22 February 2012
                Date accepted : 28 February 2012
                Categories
                Subject: Review

                Keywords: heterocycles,peptidomimetics,tricyclic compounds,scaffold
                Data availability:
                Keywords: heterocycles, peptidomimetics, tricyclic compounds, scaffold

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