Special Issue "Combinatorial Chemistry"
Deadline for manuscript submissions: closed (31 October 2009)
Dr. Lisa Marcaurelle
Broad Institute of Harvard and MIT, 7 Cambridge Center, NE30-3007, Cambridge, MA 02474, USA
Phone: +1 617 324 4374
Interests: Combinatorial chemistry, solid-phase synthesis, diversity-oriented synthesis, carbohydrates
All papers should be submitted to firstname.lastname@example.org with copy to the guest editor. To be published continuously until the deadline and papers will be listed together at the special websites.
Submitted papers should not have been previously published nor be currently under consideration for publication elsewhere. All papers are refereed through a peer review process. A guide for authors, sample copies and other relevant information for submitting papers are available on the Instructions for Authors page. Molecules is an international peer-reviewed monthly journal published by MDPI.
Please visit the Instructions for Authors page before submitting a paper. Open Access publication fees are 800 CHF per paper. English correction fees (250 CHF) will be added in certain cases (1050 CHF per paper for those papers that require extensive additional formatting and/or English corrections).
- combinatorial chemistry
- solid-phase synthesis
- diversity-oriented synthesis
Molecules 2009, 14(9), 3436-3445; doi:10.3390/molecules14093436
Received: 24 July 2009; in revised form: 10 August 2009 / Accepted: 3 September 2009 / Published: 8 September 2009| Download PDF Full-text (164 KB)
Article: Upgrading SELEX Technology by Using Lambda Exonuclease Digestion for Single-Stranded DNA Generation
Molecules 2010, 15(1), 1-11; doi:10.3390/molecules15010001
Received: 19 November 2009; in revised form: 23 December 2009 / Accepted: 23 December 2009 / Published: 24 December 2009| Download PDF Full-text (153 KB)
Article: Preparation of 16β-Estradiol Derivative Libraries as Bisubstrate Inhibitors of 17β-Hydroxysteroid Dehydrogenase Type 1 Using the Multidetachable Sulfamate Linker
Molecules 2010, 15(3), 1590-1631; doi:10.3390/molecules15031590
Received: 26 January 2010; in revised form: 8 February 2010 / Accepted: 3 March 2010 / Published: 10 March 2010| Download PDF Full-text (1264 KB)
Article: MMPBSA Decomposition of the Binding Energy throughout a Molecular Dynamics Simulation of Amyloid-Beta (Aß10−35) Aggregation
Molecules 2010, 15(4), 2730-2748; doi:10.3390/molecules15042730
Received: 13 February 2010; in revised form: 11 March 2010 / Accepted: 19 March 2010 / Published: 15 April 2010| Download PDF Full-text (901 KB)
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Manuscript ID: Molecules-combchem-20090428-us-Kurosu
Type of Paper: Review
Author: Michio Kurosu
Abstract: Perspectives on combinatorial chemistry in the development of novel bioactive molecules Review: The discovery of new small molecules that might be used as drug leads or probes to explore an increasing number of biological phenomena has long been a subject of interest. This review presents perspectives on the role of combinatorial chemistry in the discovery of bioactive small molecules. The implementation and lessons learned from the discovery of bioactive small molecules from the mid-1990s to 2009 via combinatorial chemistry and high-throughput screening methods are discussed.
Manuscript ID: molecules-combchem-20090503-il-Gilon
Title: Conversion of Peptides and Active Region in Proteins into Peptidomimetic Drug Lead Using Libraries with Conformational Diversity (Cycloscan)
Author: Chaim Gilon
Affiliation: Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel (email@example.com)
Abstract: Cycloscan is a method for the conversion of peptides and active region in proteins into peptidomimetic and macrocyclic drug leads. In cycloscan focused libraries of backbone cyclic peptides are designed based on the sequence of a bioactive linear stem peptide or on an active region (contiguous or non-contiguous) in protein. The libraries are synthesized and screened using the appropriate biological assay. The unique feature of the backbone cyclic libraries used for cycloscan is their conformational diversity. All the peptides in the libraries have the same sequence of the stem peptide and they differ from each other in the following diversity elements: (1) mode of cyclization (2) position of the ring (3) ring size (4) ring chemistry. The design of the libraries is based on hierarchical dendrimeric approach. The aim of such libraries is to explore the conformational space of the linear stem peptide by conformationally constrained backbone cyclic peptidomimetics. The libraries are screened by a combination of assays in order to select the most active, selective, metabolically stable and intestinally permeable peptidomimetic lead. The backbone cyclic peptidomimetic lead may also be converted into macrocyclic lead using the cycloscan principles. For further optimization of the peptidomimetic lead cycloscan is combined with scanning methods that do not alter the pharmacophors such: N-Me scan, chiral scan, aza scan and peptomer/peptoid scan.
The cycloscan method was applied to various linear peptides (e.g. substance P, somatostatin, GnRH, αMSH, PBAN) and to contiguous and non-contiguous active region in proteins including BPTI, CD4, Integrase, Tet, Rev).
Last update: 15 April 2010