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Special Issue "Peptidomimetics"

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A special issue of Pharmaceuticals (ISSN 1424-8247).

Deadline for manuscript submissions: closed (31 August 2011)

Special Issue Editor

Guest Editor
Prof. Dr. Andrew Abell

School of Chemistry & Physics, The University of Adelaide, North Terrace, Adelaide, SA 5005, Australia
Website | E-Mail

Published Papers (3 papers)

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Review

Open AccessReview Heterocycles in Peptidomimetics and Pseudopeptides: Design and Synthesis
Pharmaceuticals 2012, 5(3), 297-316; doi:10.3390/ph5030297
Received: 27 December 2011 / Revised: 22 February 2012 / Accepted: 28 February 2012 / Published: 8 March 2012
Cited by 7 | PDF Full-text (466 KB) | HTML Full-text | XML Full-text
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. Full article
(This article belongs to the Special Issue Peptidomimetics)
Figures

Open AccessReview Structure Based Antibody-Like Peptidomimetics
Pharmaceuticals 2012, 5(2), 209-235; doi:10.3390/ph5020209
Received: 16 December 2011 / Revised: 17 January 2012 / Accepted: 19 January 2012 / Published: 16 February 2012
Cited by 2 | PDF Full-text (665 KB) | HTML Full-text | XML Full-text
Abstract
Biologics such as monoclonal antibodies (mAb) and soluble receptors represent new classes of therapeutic agents for treatment of several diseases. High affinity and high specificity biologics can be utilized for variety of clinical purposes. Monoclonal antibodies have been used as diagnostic agents when
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Biologics such as monoclonal antibodies (mAb) and soluble receptors represent new classes of therapeutic agents for treatment of several diseases. High affinity and high specificity biologics can be utilized for variety of clinical purposes. Monoclonal antibodies have been used as diagnostic agents when coupled with radionuclide, immune modulatory agents or in the treatment of cancers. Among other limitations of using large molecules for therapy the actual cost of biologics has become an issue. There is an effort among chemists and biologists to reduce the size of biologics which includes monoclonal antibodies and receptors without a reduction of biological efficacy. Single chain antibody, camel antibodies, Fv fragments are examples of this type of deconstructive process. Small high-affinity peptides have been identified using phage screening. Our laboratory used a structure-based approach to develop small-size peptidomimetics from the three-dimensional structure of proteins with immunoglobulin folds as exemplified by CD4 and antibodies. Peptides derived either from the receptor or their cognate ligand mimics the functions of the parental macromolecule. These constrained peptides not only provide a platform for developing small molecule drugs, but also provide insight into the atomic features of protein-protein interactions. A general overview of the reduction of monoclonal antibodies to small exocyclic peptide and its prospects as a useful diagnostic and as a drug in the treatment of cancer are discussed. Full article
(This article belongs to the Special Issue Peptidomimetics)
Open AccessReview RFamide Peptides: Structure, Function, Mechanisms and Pharmaceutical Potential
Pharmaceuticals 2011, 4(9), 1248-1280; doi:10.3390/ph4091248
Received: 29 August 2011 / Revised: 9 September 2011 / Accepted: 15 September 2011 / Published: 21 September 2011
Cited by 21 | PDF Full-text (601 KB) | HTML Full-text | XML Full-text
Abstract
Different neuropeptides, all containing a common carboxy-terminal RFamide sequence, have been characterized as ligands of the RFamide peptide receptor family. Currently, five subgroups have been characterized with respect to their N-terminal sequence and hence cover a wide pattern of biological functions, like important
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Different neuropeptides, all containing a common carboxy-terminal RFamide sequence, have been characterized as ligands of the RFamide peptide receptor family. Currently, five subgroups have been characterized with respect to their N-terminal sequence and hence cover a wide pattern of biological functions, like important neuroendocrine, behavioral, sensory and automatic functions. The RFamide peptide receptor family represents a multiligand/multireceptor system, as many ligands are recognized by several GPCR subtypes within one family. Multireceptor systems are often susceptible to cross-reactions, as their numerous ligands are frequently closely related. In this review we focus on recent results in the field of structure-activity studies as well as mutational exploration of crucial positions within this GPCR system. The review summarizes the reported peptide analogs and recently developed small molecule ligands (agonists and antagonists) to highlight the current understanding of the pharmacophoric elements, required for affinity and activity at the receptor family. Furthermore, we address the biological functions of the ligands and give an overview on their involvement in physiological processes. We provide insights in the knowledge for the design of highly selective ligands for single receptor subtypes to minimize cross-talk and to eliminate effects from interactions within the GPCR system. This will support the drug development of members of the RFamide family. Full article
(This article belongs to the Special Issue Peptidomimetics)

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