Journal of Peptide Science

Cover image for Journal of Peptide Science

February 2010

Volume 16, Issue 2

Pages 81–122

  1. Research Articles

    1. Top of page
    2. Research Articles
    1. Two tachykinin-like peptides from skin secretions of Danio rerio (pages 81–84)

      Xuhua Mi, Haining Yu, Peng Jia, Zhenzhou Zhang, Luyong Zhang and Jingze Liu

      Article first published online: 3 DEC 2009 | DOI: 10.1002/psc.1194

      Two novel tachykinin-like peptides named tachykinin-DR1 and—DR2 were identified from skin secretions of Danio rerio in current work. Their amino acid sequences were determined to share a conserved FXGLM-NH2 C-terminal consensus motif. The precursor encoding both tachykinin-DR1 and—DR2 was cloned from the skin cDNA library of D. rerio, which is composed of 108 amino acid residues. Tachykinin-DRs could induce the contraction of isolated strips of guinea pig ileum just like other tackykinins.

    2. Temperature-dependent hemolytic activity of membrane pore-forming peptide toxin, tolaasin (pages 85–90)

      Kwang-Hyun Cho, Hee-Sung Wang and Young-Kee Kim

      Article first published online: 3 DEC 2009 | DOI: 10.1002/psc.1199

      Thumbnail image of graphical abstract

      The membrane binding of tolaasin is temperature-sensitive. At low temperature, tolaasin binding to erythrocyte membrane was poor and most of tolaasin molecules stayed in solution. However, membrane disruption by membrane-bound tolaasins was less sensitive to temperature change. The hemolysis was proportional to the tenth power of the amount of tolaasin, implying that tolaasin-induced hemolysis is required the multiple binding of tolaasin molecules.

    3. Study of a lipophilic captopril analogue binding to angiotensin I converting enzyme (pages 91–97)

      Georgios A. Dalkas, Damien Marchand, Jean-Claude Galleyrand, Jean Martinez, Georgios A. Spyroulias, Paul Cordopatis and Florine Cavelier

      Article first published online: 15 DEC 2009 | DOI: 10.1002/psc.1201

      Thumbnail image of graphical abstract

      The present study describes the synthesis and biological activity of Silacaptopril, a silylated analogue of known antihypertensive agent captopril, and its interaction with ACE. Docking simulations were carried out in order to study the structural characteristics and the binding properties of Silacaptopril and its analogues with ACE.

    4. Slightly modifying pseudoproline dipeptides incorporation strategy enables solid phase synthesis of a 54 AA fragment of caveolin-1 encompassing the intramembrane domain (pages 98–104)

      Yves-Marie Coïc, Charlotte Le Lan, Jean-Michel Neumann, Nadège Jamin and Françoise Baleux

      Article first published online: 15 DEC 2009 | DOI: 10.1002/psc.1203

      Thumbnail image of graphical abstract

      The synthesis of a caveolin-1 hydrophobic fragment strengthens the use of pseudoproline dipeptides as efficient tools in SPPS by avoiding a newly reported side reaction.

    5. Design, synthesis and biological activity of cell-penetrating peptide-modified octreotide analogs (pages 105–109)

      Wenlin Xie, Jian Liu, Minghua Qiu, Jiancheng Yuan and Anlong Xu

      Article first published online: 15 DEC 2009 | DOI: 10.1002/psc.1205

      Thumbnail image of graphical abstract

      Four novel octreotide analogs with Cell-Penetrating Peptide (CPPs) at the N-terminus or C-terminus were synthesized. The antiproliferative activity of the analogs was tested in vitro on human gastric (SGC-7901) and hepatocellular cancer (BEL7402) cell lines using the MTT assay. Interestingly, these analogs showed a higher anticancer activities than the parent octreotide except CMTPT03 analog. The results demonstrate that the Cell-Penetrating Peptide can enhance the anti-proliferative activity of octreotide.

    6. Nanofiber formation of amphiphilic cyclic tri-β-peptide (pages 110–114)

      Yusuke Ishihara and Shunsaku Kimura

      Article first published online: 8 JAN 2010 | DOI: 10.1002/psc.1206

      Thumbnail image of graphical abstract

      A novel amphiphilic cyclic peptide composed of two β-glucosamino acids and one trans-2-aminocyclohexylcarboxylic acid was synthesized and investigated on assembly formation. The cyclic tri-β-peptide was self-assembled into rodlike crystals or nanofibers depending on preparative conditions. In the molecular assemblies, the cyclic peptide was found to stack each other to form a columnar structure and triple bundle with homogeneous hydrogen bonds revealed by electron diffraction analysis and FT-IR measurement. Straight nanofibers with uniform diameter were also uniquely obtained.

    7. Interaction of a β-sheet breaker peptide with lipid membranes (pages 115–122)

      Giuseppe Vitiello, Manuela Grimaldi, Anna Ramunno, Ornella Ortona, Giovanni De Martino, Anna Maria D'Ursi and Gerardino D'Errico

      Article first published online: 8 JAN 2010 | DOI: 10.1002/psc.1207

      Thumbnail image of graphical abstract

      The β-sheet breaker peptide iAβ5p interacts with phospholipid membranes and this interaction is modulated by inclusion of cholesterol in the bilayer formulation. Particularly, cholesterol decreases the peptide partition coefficient between the membrane and the aqueous medium. Moreover, in the presence of cholesterol the peptide penetrates more deeply into the lipid bilayer.

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