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      Syntheses and Self-assembling Behaviors of Pentagonal Conjugates of Tryptophane Zipper-Forming Peptide

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          Abstract

          Pentagonal conjugates of tryptophane zipper-forming peptide (CKTWTWTE) with a pentaazacyclopentadecane core (Pentagonal-Gly-Trpzip and Pentagonal-Ala-Trpzip) were synthesized and their self-assembling behaviors were investigated in water. Pentagonal-Gly-Trpzip self-assembled into nanofibers with the width of about 5 nm in neutral water (pH 7) via formation of tryptophane zipper, which irreversibly converted to nanoribbons by heating. In contrast, Pentagonal-Ala-Trpzip formed irregular aggregates in water.

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          Fabrication of novel biomaterials through molecular self-assembly.

          Shuguang Zhang (2003)
          Two complementary strategies can be used in the fabrication of molecular biomaterials. In the 'top-down' approach, biomaterials are generated by stripping down a complex entity into its component parts (for example, paring a virus particle down to its capsid to form a viral cage). This contrasts with the 'bottom-up' approach, in which materials are assembled molecule by molecule (and in some cases even atom by atom) to produce novel supramolecular architectures. The latter approach is likely to become an integral part of nanomaterials manufacture and requires a deep understanding of individual molecular building blocks and their structures, assembly properties and dynamic behaviors. Two key elements in molecular fabrication are chemical complementarity and structural compatibility, both of which confer the weak and noncovalent interactions that bind building blocks together during self-assembly. Using natural processes as a guide, substantial advances have been achieved at the interface of nanomaterials and biology, including the fabrication of nanofiber materials for three-dimensional cell culture and tissue engineering, the assembly of peptide or protein nanotubes and helical ribbons, the creation of living microlenses, the synthesis of metal nanowires on DNA templates, the fabrication of peptide, protein and lipid scaffolds, the assembly of electronic materials by bacterial phage selection, and the use of radiofrequency to regulate molecular behaviors.
          Article 0 comments Cited 621 times – based on 0 reviews     Review now
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            Polyvalent Interactions in Biological Systems: Implications for Design and Use of Multivalent Ligands and Inhibitors

            Mathai Mammen, Seok-Ki Choi, George Whitesides (1998)
            Article 0 comments Cited 589 times – based on 0 reviews     Review now
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              Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization.

              Ehud Gazit (2007)
              In this tutorial review the process and applications of peptide self-assembly into nanotubes, nanospheres, nanofibrils, nanotapes, and other ordered structures at the nano-scale are discussed. The formation of well-ordered nanostructures by a process of self-association represents the essence of modern nanotechnology. Such self-assembled structures can be formed by a variety of building blocks, both organic and inorganic. Of the organic building blocks, peptides are among the most useful ones. Peptides possess the biocompatibility and chemical diversity that are found in proteins, yet they are much more stable and robust and can be readily synthesized on a large scale. Short peptides can spontaneously associate to form nanotubes, nanospheres, nanofibrils, nanotapes, and other ordered structures at the nano-scale. Peptides can also form macroscopic assemblies such as hydrogels with nano-scale order. The application of peptide building blocks in biosensors, tissue engineering, and the development of antibacterial agents has already been demonstrated.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Mol Sci
                Journal ID (publisher-id): ijms
                Title: International Journal of Molecular Sciences
                Publisher: Molecular Diversity Preservation International (MDPI)
                ISSN (Electronic): 1422-0067
                Publication date (Electronic): 15 August 2011
                Publication date Collection: 2011
                Volume: 12
                Issue: 8
                Pages: 5187-5199
                Affiliations
                [1 ] Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Moto-oka 744, Nishi-ku, Fukuoka 819-0395, Japan; E-Mails: ma2ra-k@ 123456mail.cstm.kyushu-u.ac.jp (K.M.); n-kimi@ 123456mail.cstm.kyushu-u.ac.jp (N.K.)
                [2 ] International Research Center for Molecular Systems, Kyushu University, Moto-oka 744, Nishi-ku, Fukuoka 819-0395, Japan
                Author notes
                [* ] Author to whom correspondence should be addressed; E-Mail: ma2ra-k@ 123456mail.cstm.kyushu-u.ac.jp ; Tel.: +81-92-802-2833; Fax: +81-92-802-2838.
                Article
                Publisher ID: ijms-12-05187
                DOI: 10.3390/ijms12085187
                PMC ID: 3179159
                PubMed ID: 21954352
                SO-VID: d5d0ee83-c007-4d29-a5fb-c564383023df
                Copyright © © 2011 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 : 13 June 2011
                Date revision received : 30 July 2011
                Date accepted : 10 August 2011
                Categories
                Subject: Article

                ScienceOpen disciplines: Molecular biology
                Keywords: nanofiber,pentagonal conjugate,tryptophane zipper peptide,self-assembly
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: nanofiber, pentagonal conjugate, tryptophane zipper peptide, self-assembly

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