• Issue

    Journal of Peptide Science: Volume 19, Issue 8

    461-527
    August 2013

Research Articles

Intrinsically unstructured proteins by design—electrostatic interactions can control binding, folding, and function of a helix-loop-helix heterodimer

  • Pages: 461-469
  • First Published: 27 June 2013
Intrinsically unstructured proteins by design—electrostatic interactions can control binding, folding, and function of a helix-loop-helix heterodimer

Functional heterodimeric polypeptides induced by the cooperative folding of complementary polypeptide chains have been designed, synthesized, and analyzed.

Tandem Ru-alkylidene-catalysed cross metathesis/hydrogenation: synthesis of lipophilic amino acids

  • Pages: 470-476
  • First Published: 03 June 2013
Tandem Ru-alkylidene-catalysed cross metathesis/hydrogenation: synthesis of lipophilic amino acids

Tandem catalysis with a single Ru-alkylidene pre-catalyst provides a highly generic and efficient synthesis of chiral, lipidic amino acids.

Distinct solid and solution state self-assembly pathways of RADA16-I designer peptide

  • Pages: 477-484
  • First Published: 25 June 2013
Distinct solid and solution state self-assembly pathways of RADA16-I designer peptide

Self-assembly of the RADA16-I peptide in the solid state produces β-sheets that have a structure that differs from those formed through self-assembly in the solution state. Solid state RADA16-I self-assembly produces in-register parallel β-sheets, whereas nanofibers are composed of stacked parallel β-sheets with registry shifts between adjacent β-strands. These results provide evidence for environment-dependent self-assembly mechanisms for RADA16-I β-sheets and new constraints on solid state self-assembled structures that must be avoided to maximize solution solubility and nanofiber yields.

Minimal killing unit of the mitochondrial targeting domain of Noxa

  • Pages: 485-490
  • First Published: 22 June 2013
Minimal killing unit of the mitochondrial targeting domain of Noxa

The mitochondrial targeting domain (MTD) derived from Noxa causes necrotic cell death in various cancer cells. Here, we define MTD(8) as the minimal killing unit of MTD in vitro and in vivo

Multiple antigen peptide mimetics containing gp41 membrane-proximal external region elicit broad neutralizing antibodies against human immunodeficiency virus type 1 in guinea pigs

  • Pages: 491-498
  • First Published: 21 June 2013
Multiple antigen peptide mimetics containing gp41 membrane-proximal external region elicit broad neutralizing antibodies against human immunodeficiency virus type 1 in guinea pigs

Two novel membrane-proximal external region-based MAP immunogens, 4E10- and 2F5-MAP4, were designed and broadly neutralizing antibodies against HIV-1 were induced by these two immunogens in sera of guinea pigs.

Interaction of synthetic peptide octarphin (TPLVTLFK) with human blood lymphocytes

  • Pages: 499-503
  • First Published: 23 June 2013
Interaction of synthetic peptide octarphin (TPLVTLFK) with human blood lymphocytes

The synthetic peptide octarphin, a selective agonist of non-opioid beta-endorphin receptor, binds with high affinity to human T (Image 1) and B (Image 2) lymphocytes (Kd = 3.0 and 3.2 nM, respectively). The specific binding octarphin labeled with tritium was inhibited by beta-endorphin. The opioid receptor agonists were inactive. Thus, both human blood T and B lymphocytes express non-opioid beta-endorphin receptor.

Recombinant production of TEV cleaved human parathyroid hormone

  • Pages: 504-510
  • First Published: 23 June 2013
Recombinant production of TEV cleaved human parathyroid hormone

An 1H,15N-HSQC spectrum of uniformly 15N-labeled parathyroid hormone(1-34) demonstrating the efficiency of recombinant production with a tobacco etch virus cleavable thioredoxin-fusion construct.

Localization of the anti-cancer peptide EGFR-lytic hybrid peptide in human pancreatic cancer BxPC-3 cells by immunocytochemistry

  • Pages: 511-515
  • First Published: 01 July 2013
Localization of the anti-cancer peptide EGFR-lytic hybrid peptide in human pancreatic cancer BxPC-3 cells by immunocytochemistry

Intracellular localization of EGFR-lytic hybrid peptide in BxPC-3 cells by immunocytochemistry. Green fluorescence of EGFR-lytic peptide was not detected in non-treated cells (A and D), and EGFR-lytic peptide is visible in cytoplasm in the cell treated with EGFR-lytic for 30 min (B and E) and 60 min (C and F). A number of peptides distributed around the red fluorescence of the mitochondria (E and F arrows).

Molecular dynamics simulations of certain mutant peptide models from staphylococcal nuclease reveal that initial hydrophobic collapse associated with turn propensity drives β-hairpin folding

  • Pages: 516-527
  • First Published: 21 June 2013
Molecular dynamics simulations of certain mutant peptide models from staphylococcal nuclease reveal that initial hydrophobic collapse associated with turn propensity drives β-hairpin folding

Molecular dynamics simulation study of turn mutants of β-hairpin sequence from staphylococcal nuclease protein suggests that guidance embedded in the form of β-turn propensity is essential to lead an initial hydrophobic collapsed state to a folded β-hairpin state.