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Pharmaceuticals
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Peptidomimetics
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Peptidomimetics

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

Deadline for manuscript submissions: closed (31 August 2011) | Viewed by 36504

Special Issue Editor

Prof. Dr. Andrew Abell

E-Mail Website
Guest Editor
Department of Chemistry, The University of Adelaide, North Terrace, Adelaide 5005, Australia
Interests: reversible sensors; peptidomimetics; photochemistry; electrochemical biosensors; combined imaging and sensing platforms

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Published Papers (3 papers)

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Review

466 KiB  
Review
Heterocycles in Peptidomimetics and Pseudopeptides: Design and Synthesis
by Iole Cerminara, Lucia Chiummiento, Maria Funicello, Ambra Guarnaccio and Paolo Lupattelli
Pharmaceuticals 2012, 5(3), 297-316; https://doi.org/10.3390/ph5030297 - 8 Mar 2012
Cited by 22 | Viewed by 7726
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)
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Graphical abstract

665 KiB  
Review
Structure Based Antibody-Like Peptidomimetics
by Ramachandran Murali and Mark I. Greene
Pharmaceuticals 2012, 5(2), 209-235; https://doi.org/10.3390/ph5020209 - 16 Feb 2012
Cited by 20 | Viewed by 16176
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 [...] Read more.
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)
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Figure 1

601 KiB  
Review
RFamide Peptides: Structure, Function, Mechanisms and Pharmaceutical Potential
by Maria Findeisen, Daniel Rathmann and Annette G. Beck-Sickinger
Pharmaceuticals 2011, 4(9), 1248-1280; https://doi.org/10.3390/ph4091248 - 21 Sep 2011
Cited by 65 | Viewed by 11538
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 [...] Read more.
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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