Special Issue "Chemical Protein and Peptide Synthesis"

Guest Editor
Prof. Dr. Fernando Albericio
1 Institute for Research in Biomedicine (IRB Barcelona), Parc Científic de Barcelona, Baldiri Reixac 10, 08028 Barcelona, Spain
2 School of Chemistry, University of KwaZulu-Natal, Durban 4001, South Africa
Website: http://www.pcb.ub.es/fama
E-Mail: albericio@irbbarcelona.org
Phone: +34 93 403 70 88
Fax: +34 93 403 71 26
Interests: marine natural products; bioactive natural products; peptides; solid-phase chemistry; combinatorial chemistry; drug delivery systems

Guest Editor
Dr. Thavi Govender
School of Pharmacy and Pharmacology, University of KwaZulu Natal Westville Campus, Durban 4000, South Africa
E-Mail: govenderthav@ukzn.ac.za
Interests: asymmetric catalysis; peptide chemistry and mass spectrometry

Dear Colleagues,

Today, almost hundred peptides and proteins are in the pharmaceutical world market, and much more are in several clinical phases. Although in the past the pharmaceutical industries had reduced their interest in peptide and protein research, the last decades they rekindled the interest in those chemical entities, due to novel strategy developments, advances in the areas of formulation, enhanced drug delivery technologies, and most importantly to the current chemical technological accomplishments.  The objective of this Special Issue of Molecules is to highlight the last breakthroughs in the Chemical Synthesis of Peptides and Proteins.

Prof. Dr. Fernando Albericio
Dr. Thavi Govender
Guest Editors

Submission

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• convergent synthesis
• chemical ligation
• coupling reagent
• protecting group
• resin
• solid phase synthesis
• solid support

Type of Paper: Review 
Title: Chemical Synthesis of Cystine Knots — A Promisinig Scaffold for Applications in Drug Design
Authors: Michael Reinwarth, Daichi Nasu,Harald Kolmar and Olga Avrutina 
Affiliation: Institute for Organic Chemistry and Biochemistry, TU Darmstadt, Germany
Abstract: Cystine-knot peptides, so-called knottins, display exceptional structural, thermal, and biological stability. Their eponymous motif consists of six cysteine residues forming three disulfide bonds resulting in a notably rigid structural core. Since they highly tolerate either rational or combinatoric changes in their primary structure, cystine knots are considered to be promising frameworks for peptide-based pharmaceuticals. Although knottins are available /via/chemical and recombinant routes of synthesis, head-to-tail cyclization and oxidative folding towards the respecitve bioactive isomer still are the essential steps in synthesis. Herein we report the topology of cystine knots, their synthetical availability through sploid phase peptide synthesis including postsynthetic modifications as head-to-tail cyclization and oxidative folding. Finally we describe in short recent studies on biological activity using knottins with prescribed binding characteristics to target molecules of medical relevance.